ID IPNA_EMENI Reviewed; 331 AA. AC P05326; C8VHS7; Q5BA08; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1988, sequence version 1. DT 27-MAR-2024, entry version 169. DE RecName: Full=Isopenicillin N synthase {ECO:0000303|PubMed:3319778}; DE Short=IPNS {ECO:0000303|PubMed:3319778}; DE EC=1.21.3.1 {ECO:0000269|PubMed:3319778}; GN Name=ipnA {ECO:0000303|PubMed:3319778}; Synonyms=ips; ORFNames=AN2622; OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / OS M139) (Aspergillus nidulans). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Nidulantes. OX NCBI_TaxID=227321; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND RP PATHWAY. RX PubMed=3319778; DOI=10.1016/0378-1119(87)90120-x; RA Ramon D., Carramolino L., Patino C., Sanchez F., Penalva M.A.; RT "Cloning and characterization of the isopenicillin N synthetase gene RT mediating the formation of the beta-lactam ring in Aspergillus nidulans."; RL Gene 57:171-181(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3045077; DOI=10.1128/jb.170.9.3817-3826.1988; RA Weigel B.J., Burgett S.G., Chen V.J., Skatrud P.L., Frolik C.A., RA Queener S.W., Ingolia T.D.; RT "Cloning and expression in Escherichia coli of isopenicillin N synthetase RT genes from Streptomyces lipmanii and Aspergillus nidulans."; RL J. Bacteriol. 170:3817-3826(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139; RX PubMed=16372000; DOI=10.1038/nature04341; RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.; RT "Sequencing of Aspergillus nidulans and comparative analysis with A. RT fumigatus and A. oryzae."; RL Nature 438:1105-1115(2005). RN [4] RP GENOME REANNOTATION. RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139; RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003; RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K., RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J., RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., RA Oliver S.G., Turner G.; RT "The 2008 update of the Aspergillus nidulans genome annotation: a community RT effort."; RL Fungal Genet. Biol. 46:S2-13(2009). RN [5] RP CRYSTALLIZATION. RX PubMed=7663335; DOI=10.1002/pro.5560040521; RA Roach P.L., Schofield C.J., Baldwin J.E., Clifton I.J., Hajdu J.; RT "Crystallization and preliminary X-ray diffraction studies on recombinant RT isopenicillin N synthase from Aspergillus nidulans."; RL Protein Sci. 4:1007-1009(1995). RN [6] {ECO:0007744|PDB:1IPS} RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH IRON, AND COFACTOR. RX PubMed=7791906; DOI=10.1038/375700a0; RA Roach P.L., Clifton I.J., Fueloep V., Harlos K., Barton G.J., Hajdu J., RA Andersson I., Schofield C.J., Baldwin J.E.; RT "Crystal structure of isopenicillin N synthase is the first from a new RT structural family of enzymes."; RL Nature 375:700-704(1995). RN [7] {ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1BLZ} RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH IRON AND RP N-[(5S)-5-AMINO-5-CARBOXYPENTANOYL]-L-CYSTEINYL-D-VALINE, AND COFACTOR. RX PubMed=9194566; DOI=10.1038/42990; RA Roach P.L., Clifton I.J., Hensgens C.M., Shibata N., Schofield C.J., RA Hajdu J., Baldwin J.E.; RT "Structure of isopenicillin N synthase complexed with substrate and the RT mechanism of penicillin formation."; RL Nature 387:827-830(1997). RN [8] {ECO:0007744|PDB:1QIQ, ECO:0007744|PDB:1QJE, ECO:0007744|PDB:1QJF} RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH IRON; RP N-[(5S)-5-AMINO-5-CARBOXYPENTANOYL]-L-CYSTEINYL-D-VALINE AND ISOPENICILLIN RP N, AND COFACTOR. RX PubMed=10537113; DOI=10.1038/44400; RA Burzlaff N.I., Rutledge P.J., Clifton I.J., Hensgens C.M.H., Pickford M., RA Adlington R.M., Roach P.L., Baldwin J.E.; RT "The reaction cycle of isopenicillin N synthase observed by X-ray RT diffraction."; RL Nature 401:721-724(1999). RN [9] {ECO:0007744|PDB:1HB1, ECO:0007744|PDB:1HB2, ECO:0007744|PDB:1HB3, ECO:0007744|PDB:1HB4} RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=11755401; DOI=10.1016/s1074-5521(01)00090-4; RA Ogle J.M., Clifton I.J., Rutledge P.J., Elkins J.M., Burzlaff N.I., RA Adlington R.M., Roach P.L., Baldwin J.E.; RT "Alternative oxidation by isopenicillin N synthase observed by X-ray RT diffraction."; RL Chem. Biol. 8:1231-1237(2001). RN [10] {ECO:0007744|PDB:1ODM, ECO:0007744|PDB:1ODN} RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE RP ANALOG. RX PubMed=12926272; DOI=10.1039/b212270g; RA Elkins J.M., Rutledge P.J., Burzlaff N.I., Clifton I.J., Adlington R.M., RA Roach P.L., Baldwin J.E.; RT "Crystallographic studies on the reaction of isopenicillin N synthase with RT an unsaturated substrate analogue."; RL Org. Biomol. Chem. 1:1455-1460(2003). RN [11] {ECO:0007744|PDB:1OBN, ECO:0007744|PDB:1OC1} RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE RP ANALOG. RX PubMed=12622704; DOI=10.1042/bj20021627; RA Long A.J., Clifton I.J., Roach P.L., Baldwin J.E., Schofield C.J., RA Rutledge P.J.; RT "Structural studies on the reaction of isopenicillin N synthase with the RT substrate analogue delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-alpha- RT aminobutyrate."; RL Biochem. J. 372:687-693(2003). RN [12] {ECO:0007744|PDB:1UZW} RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE RP ANALOG. RX PubMed=15175003; DOI=10.1042/bj20040529; RA Grummitt A.R., Rutledge P.J., Clifton I.J., Baldwin J.E.; RT "Active-site-mediated elimination of hydrogen fluoride from a fluorinated RT substrate analogue by isopenicillin N synthase."; RL Biochem. J. 382:659-666(2004). RN [13] {ECO:0007744|PDB:2BU9} RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE RP ANALOG. RX PubMed=16143309; DOI=10.1016/j.bbrc.2005.08.155; RA Howard-Jones A.R., Rutledge P.J., Clifton I.J., Adlington R.M., RA Baldwin J.E.; RT "Unique binding of a non-natural L,L,L-substrate by isopenicillin N RT synthase."; RL Biochem. Biophys. Res. Commun. 336:702-708(2005). RN [14] {ECO:0007744|PDB:1W03, ECO:0007744|PDB:1W04, ECO:0007744|PDB:1W05, ECO:0007744|PDB:1W06} RP X-RAY CRYSTALLOGRAPHY (1.28 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE RP ANALOG. RX PubMed=15850395; DOI=10.1021/bi047478q; RA Long A.J., Clifton I.J., Roach P.L., Baldwin J.E., Rutledge P.J., RA Schofield C.J.; RT "Structural studies on the reaction of isopenicillin N synthase with the RT truncated substrate analogues delta-(L-alpha-aminoadipoyl)-L-cysteinyl- RT glycine and delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alanine."; RL Biochemistry 44:6619-6628(2005). RN [15] {ECO:0007744|PDB:1W3V, ECO:0007744|PDB:1W3X} RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE RP ANALOG. RX PubMed=16444759; DOI=10.1002/cbic.200500282; RA Daruzzaman A., Clifton I.J., Adlington R.M., Baldwin J.E., Rutledge P.J.; RT "Unexpected oxidation of a depsipeptide substrate analogue in crystalline RT isopenicillin N synthase."; RL ChemBioChem 7:351-358(2006). RN [16] {ECO:0007744|PDB:2IVI, ECO:0007744|PDB:2IVJ} RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE RP ANALOG. RX PubMed=17397141; DOI=10.1021/bi062314q; RA Howard-Jones A.R., Elkins J.M., Clifton I.J., Roach P.L., Adlington R.M., RA Baldwin J.E., Rutledge P.J.; RT "Interactions of isopenicillin N synthase with cyclopropyl-containing RT substrate analogues reveal new mechanistic insight."; RL Biochemistry 46:4755-4762(2007). RN [17] {ECO:0007744|PDB:2JB4} RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE RP ANALOG. RX PubMed=17907118; DOI=10.1002/cbic.200700176; RA Stewart A.C., Clifton I.J., Adlington R.M., Baldwin J.E., Rutledge P.J.; RT "A cyclobutanone analogue mimics penicillin in binding to isopenicillin N RT synthase."; RL ChemBioChem 8:2003-2007(2007). RN [18] {ECO:0007744|PDB:2VAU, ECO:0007744|PDB:2VBB} RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE RP ANALOG. RX PubMed=18620394; DOI=10.1021/ja8005397; RA Ge W., Clifton I.J., Stok J.E., Adlington R.M., Baldwin J.E., RA Rutledge P.J.; RT "Isopenicillin N synthase mediates thiolate oxidation to sulfenate in a RT depsipeptide substrate analogue: implications for oxygen binding and a link RT to nitrile hydratase?"; RL J. Am. Chem. Soc. 130:10096-10102(2008). RN [19] {ECO:0007744|PDB:2VCM, ECO:0007744|PDB:2VE1} RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE RP ANALOG. RX PubMed=19598184; DOI=10.1002/cbic.200900080; RA Ge W., Clifton I.J., Howard-Jones A.R., Stok J.E., Adlington R.M., RA Baldwin J.E., Rutledge P.J.; RT "Structural studies on the reaction of isopenicillin N synthase with a RT sterically demanding depsipeptide substrate analogue."; RL ChemBioChem 10:2025-2031(2009). RN [20] {ECO:0007744|PDB:2VBP, ECO:0007744|PDB:2WO7} RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE RP ANALOG. RX PubMed=20603104; DOI=10.1016/j.bbrc.2010.06.129; RA Ge W., Clifton I.J., Stok J.E., Adlington R.M., Baldwin J.E., RA Rutledge P.J.; RT "Crystallographic studies on the binding of selectively deuterated LLD- and RT LLL-substrate epimers by isopenicillin N synthase."; RL Biochem. Biophys. Res. Commun. 398:659-664(2010). RN [21] {ECO:0007744|PDB:2VBD} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE RP ANALOG. RX PubMed=20024142; DOI=10.1039/b910170e; RA Ge W., Clifton I.J., Stok J.E., Adlington R.M., Baldwin J.E., RA Rutledge P.J.; RT "The crystal structure of an LLL-configured depsipeptide substrate analogue RT bound to isopenicillin N synthase."; RL Org. Biomol. Chem. 8:122-127(2010). RN [22] {ECO:0007744|PDB:2Y60} RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE RP ANALOG. RX PubMed=22001738; DOI=10.1016/j.abb.2011.09.014; RA Clifton I.J., Ge W., Adlington R.M., Baldwin J.E., Rutledge P.J.; RT "The crystal structure of isopenicillin N synthase with delta-((L)-alpha- RT aminoadipoyl)-(L)-cysteinyl-(D)-methionine reveals thioether coordination RT to iron."; RL Arch. Biochem. Biophys. 516:103-107(2011). RN [23] {ECO:0007744|PDB:2Y6F} RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE RP ANALOG. RX PubMed=21678539; DOI=10.1002/cbic.201100149; RA Clifton I.J., Ge W., Adlington R.M., Baldwin J.E., Rutledge P.J.; RT "Isopenicillin N synthase binds delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D- RT thia-allo-isoleucine through both sulfur atoms."; RL ChemBioChem 12:1881-1885(2011). RN [24] {ECO:0007744|PDB:4BB3} RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE RP ANALOG. RX PubMed=23262315; DOI=10.1016/j.abb.2012.12.012; RA Daruzzaman A., Clifton I.J., Adlington R.M., Baldwin J.E., Rutledge P.J.; RT "The crystal structure of isopenicillin N synthase with a dipeptide RT substrate analogue."; RL Arch. Biochem. Biophys. 530:48-53(2013). RN [25] {ECO:0007744|PDB:3ZKU, ECO:0007744|PDB:3ZKY} RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE RP ANALOGS. RX PubMed=23468426; DOI=10.1002/cbic.201200728; RA Daruzzaman A., Clifton I.J., Adlington R.M., Baldwin J.E., Rutledge P.J.; RT "The interaction of isopenicillin N synthase with homologated substrate RT analogues delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-Xaa characterised RT by protein crystallography."; RL ChemBioChem 14:599-606(2013). RN [26] {ECO:0007744|PDB:3ZOI} RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE RP ANALOG. RX PubMed=23860486; DOI=10.1016/j.febslet.2013.07.016; RA Clifton I.J., Ge W., Adlington R.M., Baldwin J.E., Rutledge P.J.; RT "The crystal structure of an isopenicillin N synthase complex with an RT ethereal substrate analogue reveals water in the oxygen binding site."; RL FEBS Lett. 587:2705-2709(2013). RN [27] {ECO:0007744|PDB:2BJS} RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 1-325 IN COMPLEX WITH IRON AND RP N-[(5S)-5-AMINO-5-CARBOXYPENTANOYL]-L-CYSTEINYL-D-VALINE, FUNCTION, RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-98; LEU-223; LEU-231; VAL-272 RP AND PRO-283. RX PubMed=28703303; DOI=10.1002/chem.201701592; RA McNeill L.A., Brown T.J.N., Sami M., Clifton I.J., Burzlaff N.I., RA Claridge T.D.W., Adlington R.M., Baldwin J.E., Rutledge P.J., RA Schofield C.J.; RT "Terminally truncated isopenicillin N synthase generates a dithioester RT product: evidence for a thioaldehyde intermediate during catalysis and a RT new mode of reaction for non-Heme iron oxidases."; RL Chemistry 23:12815-12824(2017). RN [28] {ECO:0007744|PDB:6Y0O} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS). RX PubMed=32939282; DOI=10.1107/s2052252520010374; RA Rabe P., Beale J.H., Butryn A., Aller P., Dirr A., Lang P.A., Axford D.N., RA Carr S.B., Leissing T.M., McDonough M.A., Davy B., Ebrahim A., Orlans J., RA Storm S.L.S., Orville A.M., Schofield C.J., Owen R.L.; RT "Anaerobic fixed-target serial crystallography."; RL IUCrJ 7:901-912(2020). RN [29] {ECO:0007744|PDB:6ZAK} RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE RP ANALOG. RA Rabe P., Kamps J.J.A.G., Sutherlin K., Pharm C., McDonough M.A., RA Leissing T.M., Aller P., Butryn A., Linyard J., Lang P., Brem J., RA Fuller F.D., Batyuk A., Hunter M.S., Pettinati I., Clifton I.J., RA Alonso-Mori R., Gul S., Young I., Kim I., Bhowmick A., O'Riordan L., RA Brewster A.S., Claridge T.D.W., Sauter N.K., Yachandra V., Yano J., RA Kern J.F., Orville A.M., Schofield C.J.; RT "Room temperature XFEL isopenicillin N synthase structure in complex with RT the Fe(IV)=O mimic VO and ACV."; RL Submitted (JUN-2020) to the PDB data bank. RN [30] RP X-RAY CRYSTALLOGRAPHY (1.22 ANGSTROMS) IN COMPLEX WITH IRON AND SUBSTRATE RP ANALOG. RX PubMed=34417180; DOI=10.1126/sciadv.abh0250; RA Rabe P., Kamps J.J.A.G., Sutherlin K.D., Linyard J.D.S., Aller P., RA Pham C.C., Makita H., Clifton I., McDonough M.A., Leissing T.M., Shutin D., RA Lang P.A., Butryn A., Brem J., Gul S., Fuller F.D., Kim I.S., Cheah M.H., RA Fransson T., Bhowmick A., Young I.D., O'Riordan L., Brewster A.S., RA Pettinati I., Doyle M., Joti Y., Owada S., Tono K., Batyuk A., Hunter M.S., RA Alonso-Mori R., Bergmann U., Owen R.L., Sauter N.K., Claridge T.D.W., RA Robinson C.V., Yachandra V.K., Yano J., Kern J.F., Orville A.M., RA Schofield C.J.; RT "X-ray free-electron laser studies reveal correlated motion during RT isopenicillin N synthase catalysis."; RL Sci. Adv. 7:0-0(2021). CC -!- FUNCTION: Isopenicillin N synthase; part of the gene cluster that CC mediates the biosynthesis of penicillin, the world's most important CC antibiotic (PubMed:3319778, PubMed:11755401). IpnA catalyzes the CC cyclization of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L- CC cysteinyl-D-valine (LLD-ACV or ACV) to form isopenicillin N (IPN) that CC contains the beta-lactam nucleus (PubMed:3319778, PubMed:11755401, CC PubMed:28703303). The penicillin biosynthesis occurs via 3 enzymatic CC steps, the first corresponding to the production of the tripeptide N- CC [(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) CC by the NRPS acvA. The tripeptide ACV is then cyclized to isopenicillin CC N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam CC nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for CC phenylacetic acid by the isopenicillin N acyltransferase penDE to yield CC penicillin in the peroxisomal matrix (By similarity). CC {ECO:0000250|UniProtKB:P08703, ECO:0000269|PubMed:11755401, CC ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:3319778}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 CC = 2 H2O + isopenicillin N; Xref=Rhea:RHEA:22428, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:58399, ChEBI:CHEBI:58572; EC=1.21.3.1; CC Evidence={ECO:0000269|PubMed:11755401, ECO:0000269|PubMed:28703303, CC ECO:0000269|PubMed:3319778}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22429; CC Evidence={ECO:0000269|PubMed:11755401, ECO:0000269|PubMed:28703303, CC ECO:0000269|PubMed:3319778}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00805, ECO:0000269|PubMed:10537113, CC ECO:0000269|PubMed:7791906, ECO:0000269|PubMed:9194566}; CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE- CC ProRule:PRU00805, ECO:0000269|PubMed:10537113, CC ECO:0000269|PubMed:7791906, ECO:0000269|PubMed:9194566}; CC -!- PATHWAY: Antibiotic biosynthesis; penicillin G biosynthesis; penicillin CC G from L-alpha-aminoadipate and L-cysteine and L-valine: step 2/3. CC {ECO:0000269|PubMed:3319778}. CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P05189}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P08703}. CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M18111; AAA33311.1; -; Genomic_DNA. DR EMBL; M21882; AAA33310.1; -; Genomic_DNA. DR EMBL; AACD01000045; EAA62969.1; -; Genomic_DNA. DR EMBL; BN001306; CBF84347.1; -; Genomic_DNA. DR PIR; A27355; A27355. DR RefSeq; XP_660226.1; XM_655134.1. DR PDB; 1BK0; X-ray; 1.30 A; A=1-331. DR PDB; 1BLZ; X-ray; 1.45 A; A=1-331. DR PDB; 1HB1; X-ray; 1.55 A; A=1-331. DR PDB; 1HB2; X-ray; 1.30 A; A=1-331. DR PDB; 1HB3; X-ray; 1.40 A; A=1-331. DR PDB; 1HB4; X-ray; 1.50 A; A=1-331. DR PDB; 1IPS; X-ray; 2.50 A; A/B=1-331. DR PDB; 1OBN; X-ray; 1.30 A; A=1-331. DR PDB; 1OC1; X-ray; 2.20 A; A=1-331. DR PDB; 1ODM; X-ray; 1.15 A; A=1-331. DR PDB; 1ODN; X-ray; 1.60 A; A=1-331. DR PDB; 1QIQ; X-ray; 1.50 A; A=1-331. DR PDB; 1QJE; X-ray; 1.35 A; A=1-331. DR PDB; 1QJF; X-ray; 1.40 A; A=1-331. DR PDB; 1UZW; X-ray; 1.30 A; A=1-331. DR PDB; 1W03; X-ray; 2.10 A; A=1-331. DR PDB; 1W04; X-ray; 1.28 A; A=1-331. DR PDB; 1W05; X-ray; 2.46 A; A=1-331. DR PDB; 1W06; X-ray; 1.65 A; A=1-331. DR PDB; 1W3V; X-ray; 1.40 A; A=1-331. DR PDB; 1W3X; X-ray; 1.46 A; A=1-331. DR PDB; 2BJS; X-ray; 1.30 A; A=1-325. DR PDB; 2BU9; X-ray; 1.30 A; A=1-331. DR PDB; 2IVI; X-ray; 1.30 A; B=1-331. DR PDB; 2IVJ; X-ray; 1.46 A; A=1-331. DR PDB; 2JB4; X-ray; 1.30 A; A=1-331. DR PDB; 2VAU; X-ray; 1.80 A; A=1-331. DR PDB; 2VBB; X-ray; 1.40 A; A=1-331. DR PDB; 2VBD; X-ray; 2.00 A; A=1-331. DR PDB; 2VBP; X-ray; 1.50 A; A=1-331. DR PDB; 2VCM; X-ray; 1.65 A; A=1-331. DR PDB; 2VE1; X-ray; 2.20 A; A=1-331. DR PDB; 2WO7; X-ray; 2.50 A; A=1-331. DR PDB; 2Y60; X-ray; 1.40 A; A=1-331. DR PDB; 2Y6F; X-ray; 1.79 A; A=1-331. DR PDB; 3ZKU; X-ray; 1.40 A; A=1-331. DR PDB; 3ZKY; X-ray; 1.45 A; A=1-331. DR PDB; 3ZOI; X-ray; 1.82 A; A=1-331. DR PDB; 4BB3; X-ray; 1.40 A; A=1-331. DR PDB; 6Y0O; X-ray; 2.20 A; A=1-331. DR PDB; 6Y0P; X-ray; 1.98 A; A=1-331. DR PDB; 6ZAE; X-ray; 1.40 A; A=1-331. DR PDB; 6ZAF; X-ray; 1.40 A; A=1-331. DR PDB; 6ZAG; X-ray; 1.40 A; A=1-331. DR PDB; 6ZAH; X-ray; 1.43 A; A=1-331. DR PDB; 6ZAI; X-ray; 1.55 A; A=1-331. DR PDB; 6ZAJ; X-ray; 1.53 A; A=1-331. DR PDB; 6ZAK; X-ray; 1.54 A; A=1-331. DR PDB; 6ZAL; X-ray; 1.83 A; A=1-331. DR PDB; 6ZAM; X-ray; 1.55 A; A=1-331. DR PDB; 6ZAN; X-ray; 1.35 A; A=1-331. DR PDB; 6ZAO; X-ray; 1.66 A; A=1-331. DR PDB; 6ZAP; X-ray; 1.36 A; A=1-331. DR PDB; 6ZAQ; X-ray; 1.60 A; A=1-331. DR PDB; 6ZW8; X-ray; 1.22 A; A=1-331. DR PDB; 7P3L; X-ray; 1.32 A; A=1-331. DR PDB; 7POY; X-ray; 1.75 A; A=1-331. DR PDB; 7PSW; X-ray; 1.21 A; A=1-331. DR PDB; 7ZOE; X-ray; 1.50 A; A=1-331. DR PDB; 8A4G; X-ray; 1.97 A; A=1-331. DR PDB; 8ALI; X-ray; 1.60 A; A=1-331. DR PDB; 8ALJ; X-ray; 1.68 A; A=1-331. DR PDB; 8BB9; X-ray; 1.68 A; A=1-331. DR PDB; 8BBA; X-ray; 1.50 A; A=1-331. DR PDB; 8BBB; X-ray; 1.57 A; A=1-331. DR PDB; 8BBC; X-ray; 1.71 A; A=1-331. DR PDB; 8BBD; X-ray; 1.81 A; A=1-331. DR PDBsum; 1BK0; -. DR PDBsum; 1BLZ; -. DR PDBsum; 1HB1; -. DR PDBsum; 1HB2; -. DR PDBsum; 1HB3; -. DR PDBsum; 1HB4; -. DR PDBsum; 1IPS; -. DR PDBsum; 1OBN; -. DR PDBsum; 1OC1; -. DR PDBsum; 1ODM; -. DR PDBsum; 1ODN; -. DR PDBsum; 1QIQ; -. DR PDBsum; 1QJE; -. DR PDBsum; 1QJF; -. DR PDBsum; 1UZW; -. DR PDBsum; 1W03; -. DR PDBsum; 1W04; -. DR PDBsum; 1W05; -. DR PDBsum; 1W06; -. DR PDBsum; 1W3V; -. DR PDBsum; 1W3X; -. DR PDBsum; 2BJS; -. DR PDBsum; 2BU9; -. DR PDBsum; 2IVI; -. DR PDBsum; 2IVJ; -. DR PDBsum; 2JB4; -. DR PDBsum; 2VAU; -. DR PDBsum; 2VBB; -. DR PDBsum; 2VBD; -. DR PDBsum; 2VBP; -. DR PDBsum; 2VCM; -. DR PDBsum; 2VE1; -. DR PDBsum; 2WO7; -. DR PDBsum; 2Y60; -. DR PDBsum; 2Y6F; -. DR PDBsum; 3ZKU; -. DR PDBsum; 3ZKY; -. DR PDBsum; 3ZOI; -. DR PDBsum; 4BB3; -. DR PDBsum; 6Y0O; -. DR PDBsum; 6Y0P; -. DR PDBsum; 6ZAE; -. DR PDBsum; 6ZAF; -. DR PDBsum; 6ZAG; -. DR PDBsum; 6ZAH; -. DR PDBsum; 6ZAI; -. DR PDBsum; 6ZAJ; -. DR PDBsum; 6ZAK; -. DR PDBsum; 6ZAL; -. DR PDBsum; 6ZAM; -. DR PDBsum; 6ZAN; -. DR PDBsum; 6ZAO; -. DR PDBsum; 6ZAP; -. DR PDBsum; 6ZAQ; -. DR PDBsum; 6ZW8; -. DR PDBsum; 7P3L; -. DR PDBsum; 7POY; -. DR PDBsum; 7PSW; -. DR PDBsum; 7ZOE; -. DR PDBsum; 8A4G; -. DR PDBsum; 8ALI; -. DR PDBsum; 8ALJ; -. DR PDBsum; 8BB9; -. DR PDBsum; 8BBA; -. DR PDBsum; 8BBB; -. DR PDBsum; 8BBC; -. DR PDBsum; 8BBD; -. DR AlphaFoldDB; P05326; -. DR SMR; P05326; -. DR STRING; 227321.P05326; -. DR EnsemblFungi; CBF84347; CBF84347; ANIA_02622. DR GeneID; 2874542; -. DR KEGG; ani:AN2622.2; -. DR VEuPathDB; FungiDB:AN2622; -. DR eggNOG; KOG0143; Eukaryota. DR HOGENOM; CLU_010119_6_1_1; -. DR InParanoid; P05326; -. DR OMA; EADDNAY; -. DR OrthoDB; 1057251at2759; -. DR BRENDA; 1.21.3.1; 517. DR UniPathway; UPA00149; UER00240. DR EvolutionaryTrace; P05326; -. DR Proteomes; UP000000560; Chromosome VI. DR GO; GO:0005829; C:cytosol; ISS:GO_Central. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016216; F:isopenicillin-N synthase activity; IDA:AspGD. DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW. DR GO; GO:0042318; P:penicillin biosynthetic process; IDA:AspGD. DR InterPro; IPR026992; DIOX_N. DR InterPro; IPR044861; IPNS-like_FE2OG_OXY. DR InterPro; IPR027443; IPNS-like_sf. DR InterPro; IPR002057; Isopenicillin-N_synth_CS. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1. DR Pfam; PF03171; 2OG-FeII_Oxy; 1. DR Pfam; PF14226; DIOX_N; 1. DR PRINTS; PR00682; IPNSYNTHASE. DR SUPFAM; SSF51197; Clavaminate synthase-like; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. DR PROSITE; PS00185; IPNS_1; 1. DR PROSITE; PS00186; IPNS_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic biosynthesis; Cytoplasm; Iron; Metal-binding; KW Oxidoreductase; Reference proteome; Vitamin C. FT CHAIN 1..331 FT /note="Isopenicillin N synthase" FT /id="PRO_0000219498" FT DOMAIN 176..288 FT /note="Fe2OG dioxygenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 87 FT /ligand="isopenicillin N" FT /ligand_id="ChEBI:CHEBI:58399" FT /evidence="ECO:0000269|PubMed:10537113, FT ECO:0007744|PDB:1QJE" FT BINDING 87 FT /ligand="N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D- FT valine" FT /ligand_id="ChEBI:CHEBI:58572" FT /evidence="ECO:0000269|PubMed:10537113, FT ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:9194566, FT ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1QJE, FT ECO:0007744|PDB:2BJS" FT BINDING 91 FT /ligand="isopenicillin N" FT /ligand_id="ChEBI:CHEBI:58399" FT /evidence="ECO:0000269|PubMed:10537113, FT ECO:0007744|PDB:1QJE" FT BINDING 91 FT /ligand="N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D- FT valine" FT /ligand_id="ChEBI:CHEBI:58572" FT /evidence="ECO:0000269|PubMed:10537113, FT ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:9194566, FT ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1QJE, FT ECO:0007744|PDB:2BJS" FT BINDING 183 FT /ligand="isopenicillin N" FT /ligand_id="ChEBI:CHEBI:58399" FT /evidence="ECO:0000269|PubMed:10537113, FT ECO:0007744|PDB:1QJE" FT BINDING 183 FT /ligand="N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D- FT valine" FT /ligand_id="ChEBI:CHEBI:58572" FT /evidence="ECO:0000269|PubMed:10537113, FT ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:9194566, FT ECO:0007744|PDB:1QJE, ECO:0007744|PDB:2BJS" FT BINDING 189 FT /ligand="isopenicillin N" FT /ligand_id="ChEBI:CHEBI:58399" FT /evidence="ECO:0000269|PubMed:10537113, FT ECO:0007744|PDB:1QJE" FT BINDING 189 FT /ligand="N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D- FT valine" FT /ligand_id="ChEBI:CHEBI:58572" FT /evidence="ECO:0000269|PubMed:10537113, FT ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:9194566, FT ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1QJE, FT ECO:0007744|PDB:2BJS" FT BINDING 214 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805, FT ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1BLZ, FT ECO:0007744|PDB:1HB1, ECO:0007744|PDB:1HB2, FT ECO:0007744|PDB:1HB3, ECO:0007744|PDB:1HB4, FT ECO:0007744|PDB:1OBN, ECO:0007744|PDB:1OC1, FT ECO:0007744|PDB:1ODM, ECO:0007744|PDB:1ODN, FT ECO:0007744|PDB:1QIQ, ECO:0007744|PDB:1QJE, FT ECO:0007744|PDB:1QJF, ECO:0007744|PDB:1UZW, FT ECO:0007744|PDB:1W03, ECO:0007744|PDB:1W04, FT ECO:0007744|PDB:1W05, ECO:0007744|PDB:1W06, FT ECO:0007744|PDB:1W3V, ECO:0007744|PDB:1W3X, FT ECO:0007744|PDB:2BU9, ECO:0007744|PDB:2IVI, FT ECO:0007744|PDB:2IVJ, ECO:0007744|PDB:2JB4, FT ECO:0007744|PDB:2VAU, ECO:0007744|PDB:2VBB, FT ECO:0007744|PDB:2VBD, ECO:0007744|PDB:2VBP, FT ECO:0007744|PDB:2VCM, ECO:0007744|PDB:2VE1, FT ECO:0007744|PDB:2WO7, ECO:0007744|PDB:2Y60, FT ECO:0007744|PDB:2Y6F, ECO:0007744|PDB:3ZKU, FT ECO:0007744|PDB:3ZOI, ECO:0007744|PDB:4BB3" FT BINDING 214 FT /ligand="N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D- FT valine" FT /ligand_id="ChEBI:CHEBI:58572" FT /evidence="ECO:0000269|PubMed:10537113, FT ECO:0000269|PubMed:9194566, ECO:0007744|PDB:1QJE" FT BINDING 216 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805, FT ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1BLZ, FT ECO:0007744|PDB:1HB1, ECO:0007744|PDB:1HB2, FT ECO:0007744|PDB:1HB3, ECO:0007744|PDB:1HB4, FT ECO:0007744|PDB:1OBN, ECO:0007744|PDB:1OC1, FT ECO:0007744|PDB:1ODM, ECO:0007744|PDB:1ODN, FT ECO:0007744|PDB:1QIQ, ECO:0007744|PDB:1QJE, FT ECO:0007744|PDB:1QJF, ECO:0007744|PDB:1UZW, FT ECO:0007744|PDB:1W03, ECO:0007744|PDB:1W04, FT ECO:0007744|PDB:1W05, ECO:0007744|PDB:1W06, FT ECO:0007744|PDB:1W3V, ECO:0007744|PDB:1W3X, FT ECO:0007744|PDB:2BU9, ECO:0007744|PDB:2IVI, FT ECO:0007744|PDB:2IVJ, ECO:0007744|PDB:2JB4, FT ECO:0007744|PDB:2VAU, ECO:0007744|PDB:2VBB, FT ECO:0007744|PDB:2VBD, ECO:0007744|PDB:2VBP, FT ECO:0007744|PDB:2VCM, ECO:0007744|PDB:2VE1, FT ECO:0007744|PDB:2WO7, ECO:0007744|PDB:2Y60, FT ECO:0007744|PDB:2Y6F, ECO:0007744|PDB:3ZKU, FT ECO:0007744|PDB:3ZOI, ECO:0007744|PDB:4BB3" FT BINDING 216 FT /ligand="N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D- FT valine" FT /ligand_id="ChEBI:CHEBI:58572" FT /evidence="ECO:0000269|PubMed:10537113, FT ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:9194566, FT ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1QJE, FT ECO:0007744|PDB:2BJS" FT BINDING 270 FT /ligand="Fe(2+)" FT /ligand_id="ChEBI:CHEBI:29033" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805, FT ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1BLZ, FT ECO:0007744|PDB:1HB1, ECO:0007744|PDB:1HB2, FT ECO:0007744|PDB:1HB3, ECO:0007744|PDB:1HB4, FT ECO:0007744|PDB:1OBN, ECO:0007744|PDB:1OC1, FT ECO:0007744|PDB:1ODM, ECO:0007744|PDB:1ODN, FT ECO:0007744|PDB:1QIQ, ECO:0007744|PDB:1QJE, FT ECO:0007744|PDB:1QJF, ECO:0007744|PDB:1UZW, FT ECO:0007744|PDB:1W03, ECO:0007744|PDB:1W04, FT ECO:0007744|PDB:1W05, ECO:0007744|PDB:1W06, FT ECO:0007744|PDB:1W3V, ECO:0007744|PDB:1W3X, FT ECO:0007744|PDB:2BU9, ECO:0007744|PDB:2IVI, FT ECO:0007744|PDB:2IVJ, ECO:0007744|PDB:2JB4, FT ECO:0007744|PDB:2VAU, ECO:0007744|PDB:2VBB, FT ECO:0007744|PDB:2VBD, ECO:0007744|PDB:2VBP, FT ECO:0007744|PDB:2VCM, ECO:0007744|PDB:2VE1, FT ECO:0007744|PDB:2WO7, ECO:0007744|PDB:2Y60, FT ECO:0007744|PDB:2Y6F, ECO:0007744|PDB:3ZKU, FT ECO:0007744|PDB:3ZOI, ECO:0007744|PDB:4BB3" FT BINDING 279 FT /ligand="2-oxoglutarate" FT /ligand_id="ChEBI:CHEBI:16810" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 281 FT /ligand="isopenicillin N" FT /ligand_id="ChEBI:CHEBI:58399" FT /evidence="ECO:0000269|PubMed:10537113, FT ECO:0007744|PDB:1QJE" FT BINDING 281 FT /ligand="N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D- FT valine" FT /ligand_id="ChEBI:CHEBI:58572" FT /evidence="ECO:0000269|PubMed:10537113, FT ECO:0000269|PubMed:28703303, ECO:0000269|PubMed:9194566, FT ECO:0007744|PDB:1BK0, ECO:0007744|PDB:1QJE, FT ECO:0007744|PDB:2BJS" FT SITE 211 FT /note="Transition state stabilizer" FT /evidence="ECO:0007744|PDB:1QJE" FT MUTAGEN 98 FT /note="K->E: Strongly reduced the catalytic activity." FT /evidence="ECO:0000269|PubMed:28703303" FT MUTAGEN 223 FT /note="L->I,V: Strongly reduced the catalytic activity." FT /evidence="ECO:0000269|PubMed:28703303" FT MUTAGEN 231 FT /note="L->I,V: Strongly reduced the catalytic activity." FT /evidence="ECO:0000269|PubMed:28703303" FT MUTAGEN 231 FT /note="L->T: Abolishes the catalytic activity." FT /evidence="ECO:0000269|PubMed:28703303" FT MUTAGEN 272 FT /note="V->T: Strongly reduced the catalytic activity." FT /evidence="ECO:0000269|PubMed:28703303" FT MUTAGEN 283 FT /note="P->A,I,V: Strongly reduced the catalytic activity." FT /evidence="ECO:0000269|PubMed:28703303" FT MUTAGEN 283 FT /note="P->L: Abolishes the catalytic activity." FT /evidence="ECO:0000269|PubMed:28703303" FT STRAND 11..13 FT /evidence="ECO:0007829|PDB:1ODM" FT HELIX 15..18 FT /evidence="ECO:0007829|PDB:1ODM" FT HELIX 22..37 FT /evidence="ECO:0007829|PDB:1ODM" FT STRAND 40..46 FT /evidence="ECO:0007829|PDB:1ODM" FT HELIX 51..64 FT /evidence="ECO:0007829|PDB:1ODM" FT HELIX 67..73 FT /evidence="ECO:0007829|PDB:1ODM" FT TURN 76..78 FT /evidence="ECO:0007829|PDB:1ODM" FT STRAND 86..91 FT /evidence="ECO:0007829|PDB:1ODM" FT TURN 95..97 FT /evidence="ECO:0007829|PDB:1ODM" FT STRAND 101..105 FT /evidence="ECO:0007829|PDB:1ODM" FT HELIX 115..118 FT /evidence="ECO:0007829|PDB:1ODM" FT TURN 132..134 FT /evidence="ECO:0007829|PDB:1ODM" FT HELIX 138..163 FT /evidence="ECO:0007829|PDB:1ODM" FT TURN 168..171 FT /evidence="ECO:0007829|PDB:1ODM" FT HELIX 172..174 FT /evidence="ECO:0007829|PDB:1ODM" FT TURN 177..179 FT /evidence="ECO:0007829|PDB:1ODM" FT STRAND 183..189 FT /evidence="ECO:0007829|PDB:1ODM" FT HELIX 197..199 FT /evidence="ECO:0007829|PDB:1ODM" FT STRAND 208..214 FT /evidence="ECO:0007829|PDB:1ODM" FT STRAND 217..225 FT /evidence="ECO:0007829|PDB:1ODM" FT STRAND 231..235 FT /evidence="ECO:0007829|PDB:1ODM" FT STRAND 238..241 FT /evidence="ECO:0007829|PDB:1ODM" FT STRAND 248..253 FT /evidence="ECO:0007829|PDB:1ODM" FT HELIX 255..260 FT /evidence="ECO:0007829|PDB:1ODM" FT TURN 261..263 FT /evidence="ECO:0007829|PDB:1ODM" FT STRAND 270..273 FT /evidence="ECO:0007829|PDB:1ODM" FT STRAND 279..286 FT /evidence="ECO:0007829|PDB:1ODM" FT STRAND 301..303 FT /evidence="ECO:0007829|PDB:6ZAQ" FT HELIX 313..328 FT /evidence="ECO:0007829|PDB:1ODM" SQ SEQUENCE 331 AA; 37522 MW; 5BA1A726E9EEFA25 CRC64; MGSVSKANVP KIDVSPLFGD DQAAKMRVAQ QIDAASRDTG FFYAVNHGIN VQRLSQKTKE FHMSITPEEK WDLAIRAYNK EHQDQVRAGY YLSIPGKKAV ESFCYLNPNF TPDHPRIQAK TPTHEVNVWP DETKHPGFQD FAEQYYWDVF GLSSALLKGY ALALGKEENF FARHFKPDDT LASVVLIRYP YLDPYPEAAI KTAADGTKLS FEWHEDVSLI TVLYQSNVQN LQVETAAGYQ DIEADDTGYL INCGSYMAHL TNNYYKAPIH RVKWVNAERQ SLPFFVNLGY DSVIDPFDPR EPNGKSDREP LSYGDYLQNG LVSLINKNGQ T //