ID PPSC_MYCTU Reviewed; 2188 AA. AC P96202; L0TBB0; DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 2. DT 27-MAR-2024, entry version 168. DE RecName: Full=Phenolphthiocerol/phthiocerol polyketide synthase subunit C {ECO:0000305}; DE EC=2.3.1.292 {ECO:0000269|PubMed:15749014, ECO:0000305|PubMed:20553505}; DE AltName: Full=(Phenol)carboxyphthiodiolenone synthase subunit C; DE AltName: Full=Beta-ketoacyl-acyl-carrier-protein synthase I; DE AltName: Full=Phthiocerol synthesis polyketide synthase type I PpsC; GN Name=ppsC; OrderedLocusNames=Rv2933; OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=83332; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., RA Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the complete RT genome sequence."; RL Nature 393:537-544(1998). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY. RX PubMed=15749014; DOI=10.1016/j.molcel.2005.02.009; RA Trivedi O.A., Arora P., Vats A., Ansari M.Z., Tickoo R., Sridharan V., RA Mohanty D., Gokhale R.S.; RT "Dissecting the mechanism and assembly of a complex virulence mycobacterial RT lipid."; RL Mol. Cell 17:631-643(2005). RN [3] RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS]. RX PubMed=19099550; DOI=10.1186/1752-0509-2-109; RA Raman K., Yeturu K., Chandra N.; RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis RT through an interactome, reactome and genome-scale structural analysis."; RL BMC Syst. Biol. 2:109-109(2008). RN [4] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=20553505; DOI=10.1111/j.1742-464x.2010.07688.x; RA Simeone R., Leger M., Constant P., Malaga W., Marrakchi H., Daffe M., RA Guilhot C., Chalut C.; RT "Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis RT of phthiocerol dimycocerosates and related compounds in Mycobacterium RT tuberculosis."; RL FEBS J. 277:2715-2725(2010). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=21969609; DOI=10.1074/mcp.m111.011445; RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K., RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R., RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M., RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.; RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution RT mass spectrometry."; RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011). RN [6] RP PHOSPHOPANTETHEINYLATION AT SER-2105, AND MUTAGENESIS OF SER-2105. RX PubMed=28203522; DOI=10.1002/2211-5463.12140; RA Jung J., Bashiri G., Johnston J.M., Baker E.N.; RT "Mass spectral determination of phosphopantetheinylation specificity for RT carrier proteins in Mycobacterium tuberculosis."; RL FEBS Open Bio 6:1220-1226(2016). RN [7] {ECO:0007744|PDB:1PQW} RP X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) OF 1559-1755, AND SUBUNIT. RC STRAIN=ATCC 25618 / H37Rv; RA Gogos A., Mu H., Shapiro L.; RT "Putative enoyl reductase domain of polyketide synthase."; RL Submitted (JUN-2003) to the PDB data bank. RN [8] {ECO:0007744|PDB:4OKI, ECO:0007744|PDB:4OOC} RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1558-1750. RA Faille A., Slama N., Quemard A., Mourey L., Pedelacq J.D.; RT "Insights into the catalytic mechanism of the DH domain of the RT Mycobacterium tuberculosis polyketide synthase PpsC and architecture of the RT beta-carbon processing domains."; RL Submitted (JAN-2014) to the PDB data bank. RN [9] {ECO:0007744|PDB:5I0K, ECO:0007744|PDB:5L84, ECO:0007744|PDB:5NJI} RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 921-1217 OF APOENZYME AND IN RP COMPLEXES WITH TRANS-BUT-2-ENOYL-COA AND TRANS-DODEC-2-ENOYL-COA RP DERIVATIVES, ACTIVE SITE, AND MUTAGENESIS OF HIS-959. RX PubMed=28377293; DOI=10.1016/j.jmb.2017.03.026; RA Faille A., Gavalda S., Slama N., Lherbet C., Maveyraud L., Guillet V., RA Laval F., Quemard A., Mourey L., Pedelacq J.D.; RT "Insights into substrate modification by dehydratases from type I RT polyketide synthases."; RL J. Mol. Biol. 429:1554-1569(2017). CC -!- FUNCTION: Part of the PpsABCDE complex involved in the biosynthesis of CC the lipid core common to phthiocerols and phenolphthiocerols by CC successive additions of malonyl-CoA or methylmalonyl-CoA extender units CC (PubMed:15749014, PubMed:20553505). PpsA can accept as substrate the CC activated forms of either icosanoyl (C20), docosanoyl (C22) or CC lignoceroyl (C24) groups from FadD26, or a (4-hydroxyphenyl)-C17 or (4- CC hydroxyphenyl)-C19 fatty acyl from FadD29 (PubMed:15749014, CC PubMed:20553505). PpsA initiates the biosynthesis and extends its CC substrate using a malonyl-CoA extender unit. The PpsB and PpsC proteins CC add the second and third malonyl-CoA extender units. PpsD adds an (R)- CC methylmalonyl unit and PpsE adds a second (R)-methylmalonyl unit. The CC incorporation of the methylmalonyl units results in formation of two CC branched methyl groups in the elongated product (PubMed:15749014). CC {ECO:0000269|PubMed:15749014, ECO:0000269|PubMed:20553505}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 (S)-methylmalonyl-CoA + 10 H(+) + icosanoyl- CC [(phenol)carboxyphthiodiolenone synthase] + 3 malonyl-CoA + 5 NADPH = CC C32-carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone synthase] CC + 5 CO2 + 5 CoA + 2 H2O + 5 NADP(+); Xref=Rhea:RHEA:57748, Rhea:RHEA- CC COMP:14985, Rhea:RHEA-COMP:14986, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57327, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:87848, ChEBI:CHEBI:142236; CC EC=2.3.1.292; Evidence={ECO:0000269|PubMed:15749014, CC ECO:0000305|PubMed:20553505}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 (S)-methylmalonyl-CoA + docosanoyl- CC [(phenol)carboxyphthiodiolenone synthase] + 10 H(+) + 3 malonyl-CoA + CC 5 NADPH = C34-carboxyphthiodiolenone-[(phenol)carboxyphthiodiolenone CC synthase] + 5 CO2 + 5 CoA + 2 H2O + 5 NADP(+); Xref=Rhea:RHEA:57752, CC Rhea:RHEA-COMP:14987, Rhea:RHEA-COMP:14988, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57327, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:142237, ChEBI:CHEBI:142238; CC EC=2.3.1.292; Evidence={ECO:0000269|PubMed:15749014, CC ECO:0000305|PubMed:20553505}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 (S)-methylmalonyl-CoA + 17-(4-hydroxyphenyl)heptadecanoyl- CC [(phenol)carboxyphthiodiolenone synthase] + 10 H(+) + 3 malonyl-CoA + CC 5 NADPH = C35-(phenol)carboxyphthiodiolenone- CC [(phenol)carboxyphthiodiolenone synthase] + 5 CO2 + 5 CoA + 2 H2O + 5 CC NADP(+); Xref=Rhea:RHEA:57756, Rhea:RHEA-COMP:14272, Rhea:RHEA- CC COMP:14989, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57327, ChEBI:CHEBI:57384, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133300, CC ChEBI:CHEBI:142259; EC=2.3.1.292; CC Evidence={ECO:0000269|PubMed:15749014, ECO:0000305|PubMed:20553505}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2 (S)-methylmalonyl-CoA + 19-(4-hydroxyphenyl)nonadecanoyl- CC [(phenol)carboxyphthiodiolenone synthase] + 10 H(+) + 3 malonyl-CoA + CC 5 NADPH = C37-(phenol)carboxyphthiodiolenone- CC [(phenol)carboxyphthiodiolenone synthase] + 5 CO2 + 5 CoA + 2 H2O + 5 CC NADP(+); Xref=Rhea:RHEA:57760, Rhea:RHEA-COMP:14273, Rhea:RHEA- CC COMP:14990, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57327, ChEBI:CHEBI:57384, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:133301, CC ChEBI:CHEBI:142260; EC=2.3.1.292; CC Evidence={ECO:0000269|PubMed:15749014, ECO:0000305|PubMed:20553505}; CC -!- COFACTOR: CC Name=NADP(+); Xref=ChEBI:CHEBI:58349; CC Evidence={ECO:0000269|PubMed:15749014}; CC -!- COFACTOR: CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; CC Evidence={ECO:0000269|PubMed:28203522}; CC Note=Binds 1 phosphopantetheine covalently. CC {ECO:0000305|PubMed:28203522}; CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000269|PubMed:15749014}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.7}. CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target. CC {ECO:0000269|PubMed:19099550}. 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; AL123456; CCP45736.1; -; Genomic_DNA. DR PIR; A70984; A70984. DR RefSeq; NP_217449.1; NC_000962.3. DR RefSeq; WP_003414837.1; NZ_KK339370.1. DR PDB; 1PQW; X-ray; 2.66 A; A/B=1559-1755. DR PDB; 4OKI; X-ray; 1.50 A; A/B=1558-1750. DR PDB; 4OOC; X-ray; 2.70 A; A=921-1222. DR PDB; 5I0K; X-ray; 3.20 A; A=921-1217. DR PDB; 5L84; X-ray; 2.90 A; A=921-1222. DR PDB; 5NJI; X-ray; 1.60 A; A=921-1222. DR PDB; 6RCX; X-ray; 2.00 A; B=2057-2188. DR PDB; 7AHB; X-ray; 1.90 A; A/B=546-876. DR PDB; 7BDW; X-ray; 2.55 A; B=2060-2188. DR PDBsum; 1PQW; -. DR PDBsum; 4OKI; -. DR PDBsum; 4OOC; -. DR PDBsum; 5I0K; -. DR PDBsum; 5L84; -. DR PDBsum; 5NJI; -. DR PDBsum; 6RCX; -. DR PDBsum; 7AHB; -. DR PDBsum; 7BDW; -. DR AlphaFoldDB; P96202; -. DR SMR; P96202; -. DR STRING; 83332.Rv2933; -. DR iPTMnet; P96202; -. DR PaxDb; 83332-Rv2933; -. DR GeneID; 887686; -. DR KEGG; mtu:Rv2933; -. DR PATRIC; fig|83332.111.peg.3263; -. DR TubercuList; Rv2933; -. DR eggNOG; COG0604; Bacteria. DR eggNOG; COG1028; Bacteria. DR eggNOG; COG3321; Bacteria. DR InParanoid; P96202; -. DR OrthoDB; 9778690at2; -. DR PhylomeDB; P96202; -. DR UniPathway; UPA00094; -. DR EvolutionaryTrace; P96202; -. DR Proteomes; UP000001584; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; HDA:MTBBASE. DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE. DR GO; GO:0034081; C:polyketide synthase complex; ISS:UniProtKB. DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro. DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro. DR GO; GO:0071766; P:Actinobacterium-type cell wall biogenesis; ISS:UniProtKB. DR GO; GO:0071770; P:DIM/DIP cell wall layer assembly; IDA:MTBBASE. DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:MTBBASE. DR GO; GO:0097041; P:phenolic phthiocerol biosynthetic process; ISS:UniProtKB. DR GO; GO:0097040; P:phthiocerol biosynthetic process; ISS:UniProtKB. DR CDD; cd05195; enoyl_red; 1. DR CDD; cd00833; PKS; 1. DR Gene3D; 3.40.47.10; -; 1. DR Gene3D; 1.10.1200.10; ACP-like; 1. DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1. DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1. DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3. DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1. DR InterPro; IPR001227; Ac_transferase_dom_sf. DR InterPro; IPR036736; ACP-like_sf. DR InterPro; IPR014043; Acyl_transferase. DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase. DR InterPro; IPR013154; ADH-like_N. DR InterPro; IPR011032; GroES-like_sf. DR InterPro; IPR018201; Ketoacyl_synth_AS. DR InterPro; IPR014031; Ketoacyl_synth_C. DR InterPro; IPR014030; Ketoacyl_synth_N. DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom. DR InterPro; IPR042104; PKS_dehydratase_sf. DR InterPro; IPR020807; PKS_DH. DR InterPro; IPR049551; PKS_DH_C. DR InterPro; IPR049552; PKS_DH_N. DR InterPro; IPR020843; PKS_ER. DR InterPro; IPR013968; PKS_KR. DR InterPro; IPR020806; PKS_PP-bd. DR InterPro; IPR009081; PP-bd_ACP. DR InterPro; IPR006162; Ppantetheine_attach_site. DR InterPro; IPR016039; Thiolase-like. DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1. DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1. DR Pfam; PF00698; Acyl_transf_1; 1. DR Pfam; PF08240; ADH_N; 1. DR Pfam; PF13602; ADH_zinc_N_2; 1. DR Pfam; PF00109; ketoacyl-synt; 1. DR Pfam; PF02801; Ketoacyl-synt_C; 1. DR Pfam; PF08659; KR; 1. DR Pfam; PF21089; PKS_DH_N; 1. DR Pfam; PF00550; PP-binding; 1. DR Pfam; PF14765; PS-DH; 1. DR SMART; SM00827; PKS_AT; 1. DR SMART; SM00826; PKS_DH; 1. DR SMART; SM00829; PKS_ER; 1. DR SMART; SM00822; PKS_KR; 1. DR SMART; SM00825; PKS_KS; 1. DR SMART; SM00823; PKS_PP; 1. DR SUPFAM; SSF47336; ACP-like; 1. DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1. DR SUPFAM; SSF50129; GroES-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3. DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1. DR SUPFAM; SSF53901; Thiolase-like; 1. DR PROSITE; PS50075; CARRIER; 1. DR PROSITE; PS00606; KS3_1; 1. DR PROSITE; PS52004; KS3_2; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1. DR PROSITE; PS52019; PKS_MFAS_DH; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Fatty acid metabolism; Lipid metabolism; KW Multifunctional enzyme; NADP; Oxidoreductase; Phosphopantetheine; KW Phosphoprotein; Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:21969609" FT CHAIN 2..2188 FT /note="Phenolphthiocerol/phthiocerol polyketide synthase FT subunit C" FT /id="PRO_0000406948" FT DOMAIN 34..462 FT /note="Ketosynthase family 3 (KS3)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT DOMAIN 928..1223 FT /note="PKS/mFAS DH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363" FT DOMAIN 2069..2145 FT /note="Carrier" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258" FT REGION 572..890 FT /note="Acyltransferase" FT /evidence="ECO:0000250" FT REGION 928..1093 FT /note="Dehydratase" FT /evidence="ECO:0000250" FT REGION 928..1050 FT /note="N-terminal hotdog fold" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363" FT REGION 1067..1223 FT /note="C-terminal hotdog fold" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363" FT REGION 1467..1778 FT /note="Enoylreductase" FT /evidence="ECO:0000250" FT REGION 1802..1981 FT /note="Beta-ketoacyl reductase" FT /evidence="ECO:0000250" FT ACT_SITE 210 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 345 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 384 FT /note="For beta-ketoacyl synthase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01348" FT ACT_SITE 660 FT /note="For malonyltransferase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022" FT ACT_SITE 959 FT /note="Proton acceptor; for dehydratase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363, FT ECO:0000305|PubMed:28377293" FT ACT_SITE 1129 FT /note="Proton donor; for dehydratase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01363" FT BINDING 1803..1848 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylthreonine" FT /evidence="ECO:0007744|PubMed:21969609" FT MOD_RES 2105 FT /note="O-(pantetheine 4'-phosphoryl)serine" FT /evidence="ECO:0000269|PubMed:28203522" FT MUTAGEN 959 FT /note="H->F: Lack of dehydration reaction." FT /evidence="ECO:0000269|PubMed:28377293" FT MUTAGEN 2105 FT /note="S->A: Lack of phosphopantetheinylation." FT /evidence="ECO:0000269|PubMed:28203522" FT HELIX 546..551 FT /evidence="ECO:0007829|PDB:7AHB" FT STRAND 571..575 FT /evidence="ECO:0007829|PDB:7AHB" FT TURN 583..586 FT /evidence="ECO:0007829|PDB:7AHB" FT HELIX 587..592 FT /evidence="ECO:0007829|PDB:7AHB" FT HELIX 594..611 FT /evidence="ECO:0007829|PDB:7AHB" FT HELIX 615..620 FT /evidence="ECO:0007829|PDB:7AHB" FT HELIX 628..648 FT /evidence="ECO:0007829|PDB:7AHB" FT STRAND 654..658 FT /evidence="ECO:0007829|PDB:7AHB" FT HELIX 660..662 FT /evidence="ECO:0007829|PDB:7AHB" FT HELIX 663..669 FT /evidence="ECO:0007829|PDB:7AHB" FT HELIX 675..689 FT /evidence="ECO:0007829|PDB:7AHB" FT HELIX 690..692 FT /evidence="ECO:0007829|PDB:7AHB" FT STRAND 697..703 FT /evidence="ECO:0007829|PDB:7AHB" FT HELIX 705..711 FT /evidence="ECO:0007829|PDB:7AHB" FT TURN 712..714 FT /evidence="ECO:0007829|PDB:7AHB" FT STRAND 719..723 FT /evidence="ECO:0007829|PDB:7AHB" FT STRAND 725..727 FT /evidence="ECO:0007829|PDB:7AHB" FT STRAND 729..733 FT /evidence="ECO:0007829|PDB:7AHB" FT HELIX 735..747 FT /evidence="ECO:0007829|PDB:7AHB" FT STRAND 752..754 FT /evidence="ECO:0007829|PDB:7AHB" FT HELIX 764..769 FT /evidence="ECO:0007829|PDB:7AHB" FT HELIX 770..776 FT /evidence="ECO:0007829|PDB:7AHB" FT TURN 777..779 FT /evidence="ECO:0007829|PDB:7AHB" FT STRAND 789..794 FT /evidence="ECO:0007829|PDB:7AHB" FT TURN 795..798 FT /evidence="ECO:0007829|PDB:7AHB" FT STRAND 801..803 FT /evidence="ECO:0007829|PDB:7AHB" FT HELIX 809..817 FT /evidence="ECO:0007829|PDB:7AHB" FT HELIX 822..830 FT /evidence="ECO:0007829|PDB:7AHB" FT STRAND 835..838 FT /evidence="ECO:0007829|PDB:7AHB" FT STRAND 840..842 FT /evidence="ECO:0007829|PDB:7AHB" FT HELIX 846..856 FT /evidence="ECO:0007829|PDB:7AHB" FT HELIX 859..861 FT /evidence="ECO:0007829|PDB:7AHB" FT STRAND 863..865 FT /evidence="ECO:0007829|PDB:7AHB" FT TURN 929..931 FT /evidence="ECO:0007829|PDB:5NJI" FT STRAND 933..936 FT /evidence="ECO:0007829|PDB:5NJI" FT TURN 938..940 FT /evidence="ECO:0007829|PDB:5NJI" FT STRAND 943..949 FT /evidence="ECO:0007829|PDB:5NJI" FT HELIX 956..958 FT /evidence="ECO:0007829|PDB:5NJI" FT STRAND 959..961 FT /evidence="ECO:0007829|PDB:5NJI" FT STRAND 964..966 FT /evidence="ECO:0007829|PDB:5NJI" FT HELIX 969..983 FT /evidence="ECO:0007829|PDB:5NJI" FT STRAND 987..990 FT /evidence="ECO:0007829|PDB:5NJI" FT STRAND 992..999 FT /evidence="ECO:0007829|PDB:5NJI" FT STRAND 1009..1017 FT /evidence="ECO:0007829|PDB:5NJI" FT STRAND 1019..1029 FT /evidence="ECO:0007829|PDB:5NJI" FT STRAND 1031..1033 FT /evidence="ECO:0007829|PDB:4OOC" FT STRAND 1035..1045 FT /evidence="ECO:0007829|PDB:5NJI" FT STRAND 1067..1070 FT /evidence="ECO:0007829|PDB:5NJI" FT HELIX 1072..1081 FT /evidence="ECO:0007829|PDB:5NJI" FT STRAND 1084..1086 FT /evidence="ECO:0007829|PDB:5NJI" FT HELIX 1088..1090 FT /evidence="ECO:0007829|PDB:5NJI" FT STRAND 1093..1099 FT /evidence="ECO:0007829|PDB:5NJI" FT STRAND 1100..1102 FT /evidence="ECO:0007829|PDB:5L84" FT STRAND 1104..1108 FT /evidence="ECO:0007829|PDB:5NJI" FT HELIX 1112..1114 FT /evidence="ECO:0007829|PDB:5NJI" FT TURN 1115..1117 FT /evidence="ECO:0007829|PDB:5NJI" FT HELIX 1118..1120 FT /evidence="ECO:0007829|PDB:4OOC" FT HELIX 1125..1133 FT /evidence="ECO:0007829|PDB:5NJI" FT HELIX 1134..1137 FT /evidence="ECO:0007829|PDB:5NJI" FT HELIX 1139..1145 FT /evidence="ECO:0007829|PDB:5NJI" FT STRAND 1161..1171 FT /evidence="ECO:0007829|PDB:5NJI" FT HELIX 1175..1177 FT /evidence="ECO:0007829|PDB:5NJI" FT STRAND 1180..1188 FT /evidence="ECO:0007829|PDB:5NJI" FT STRAND 1191..1199 FT /evidence="ECO:0007829|PDB:5NJI" FT STRAND 1205..1216 FT /evidence="ECO:0007829|PDB:5NJI" FT HELIX 1572..1587 FT /evidence="ECO:0007829|PDB:4OKI" FT TURN 1588..1591 FT /evidence="ECO:0007829|PDB:4OKI" FT STRAND 1598..1601 FT /evidence="ECO:0007829|PDB:4OKI" FT TURN 1602..1605 FT /evidence="ECO:0007829|PDB:4OKI" FT HELIX 1607..1619 FT /evidence="ECO:0007829|PDB:4OKI" FT STRAND 1622..1629 FT /evidence="ECO:0007829|PDB:4OKI" FT HELIX 1630..1638 FT /evidence="ECO:0007829|PDB:4OKI" FT STRAND 1642..1646 FT /evidence="ECO:0007829|PDB:4OKI" FT HELIX 1652..1659 FT /evidence="ECO:0007829|PDB:4OKI" FT TURN 1660..1662 FT /evidence="ECO:0007829|PDB:4OKI" FT STRAND 1665..1670 FT /evidence="ECO:0007829|PDB:4OKI" FT HELIX 1675..1682 FT /evidence="ECO:0007829|PDB:4OKI" FT STRAND 1684..1692 FT /evidence="ECO:0007829|PDB:4OKI" FT HELIX 1696..1699 FT /evidence="ECO:0007829|PDB:4OKI" FT STRAND 1703..1705 FT /evidence="ECO:0007829|PDB:4OKI" FT HELIX 1706..1709 FT /evidence="ECO:0007829|PDB:4OKI" FT TURN 1710..1712 FT /evidence="ECO:0007829|PDB:4OKI" FT STRAND 1714..1717 FT /evidence="ECO:0007829|PDB:4OKI" FT HELIX 1720..1726 FT /evidence="ECO:0007829|PDB:4OKI" FT HELIX 1728..1743 FT /evidence="ECO:0007829|PDB:4OKI" FT HELIX 2073..2086 FT /evidence="ECO:0007829|PDB:6RCX" FT HELIX 2098..2101 FT /evidence="ECO:0007829|PDB:6RCX" FT HELIX 2105..2119 FT /evidence="ECO:0007829|PDB:6RCX" FT HELIX 2127..2130 FT /evidence="ECO:0007829|PDB:6RCX" FT HELIX 2134..2144 FT /evidence="ECO:0007829|PDB:6RCX" SQ SEQUENCE 2188 AA; 230622 MW; 3C431C011F01F1A2 CRC64; MTAATPDRRA IITEALHKID DLTARLEIAE KSSSEPIAVI GMGCRFPGGV NNPEQFWDLL CAGRSGIVRV PAQRWDADAY YCDDHTVPGT ICSTEGGFLT SWQPDEFDAE FFSISPREAA AMDPQQRLLI EVAWEALEDA GVPQHTIRGT QTSVFVGVTA YDYMLTLAGR LRPVDLDAYI PTGNSANFAA GRLAYILGAR GPAVVIDTAC SSSLVAVHLA CQSLRGRESD MALVGGTNLL LSPGPSIACS RWGMLSPEGR CKTFDASADG YVRGEGAAVV VLKRLDDAVR DGNRILAVVR GSAVNQDGAS SGVTVPNGPA QQALLAKALT SSKLTAADID YVEAHGTGTP LGDPIELDSL SKVFSDRAGS DQLVIGSVKT NLGHLEAAAG VAGLMKAVLA VHNGYIPRHL NFHQLTPHAS EAASRLRIAA DGIDWPTTGR PRRAGVSSFG VSGTNAHVVI EQAPDPMAAA GTEPQRGPVP AVSTLVVFGK TAPRVAATAS VLADWLDGPG AAVPLADVAH TLNHHRARQT RFGTVAAVDR RQAVIGLRAL AAGQSAPGVV APREGSIGGG TVFVYSGRGS QWAGMGRQLL ADEPAFAAAI AELEPEFVAQ GGFSLRDVIA GGKELVGIEQ IQLGLIGMQL ALTALWRSYG VTPDAVIGHS MGEVAAAVVA GALTPAQGLR VTAVRSRLMA PLSGQGTMAL LELDAEATEA LIADYPEVSL GIYASPRQTV ISGPPLLIDE LIDKVRQQNG FATRVNIEVA PHNPAMDALQ PAMRSELADL TPQPPTIPII STTYADLGIS LGSGPRFDAE HWATNMRNPV RFHQAIAHAG ADHHTFIEIS AHPLLTHSIS DTLRASYDVD NYLSIGTLQR DAHDTLEFHT NLNTTHTTHP PQTPHPPEPH PVLPTTPWQH TQHWITATSA AYHRPDTHPL LGVGVTDPTN GTRVWESELD PDLLWLADHV IDDLVVLPGA AYAEIALAAA TDTFAVEQDQ PWMISELDLR QMLHVTPGTV LVTTLTGDEQ RCQVEIRTRS GSSGWTTHAT ATVARAEPLA PLDHEGQRRE VTTADLEDQL DPDDLYQRLR GAGQQHGPAF QGIVGLAVTQ AGVARAQVRL PASARTGSRE FMLHPVMMDI ALQTLGATRT ATDLAGGQDA RQGPSSNSAL VVPVRFAGVH VYGDITRGVR AVGSLAAAGD RLVGEVVLTD ANGQPLLVVD EVEMAVLGSG SGATELTNRL FMLEWEPAPL EKTAEATGAL LLIGDPAAGD PLLPALQSSL RDRITDLELA SAADEATLRA AISRTSWDGI VVVCPPRAND ESMPDEAQLE LARTRTLLVA SVVETVTRMG ARKSPRLWIV TRGAAQFDAG ESVTLAQTGL RGIARVLTFE HSELNTTLVD IEPDGTGSLA ALAEELLAGS EADEVALRDG QRYVNRLVPA PTTTSGDLAA EARHQVVNLD SSGASRAAVR LQIDQPGRLD ALNVHEVKRG RPQGDQVEVR VVAAGLNFSD VLKAMGVYPG LDGAAPVIGG ECVGYVTAIG DEVDGVEVGQ RVIAFGPGTF GTHLGTIADL VVPIPDTLAD NEAATFGVAY LTAWHSLCEV GRLSPGERVL IHSATGGVGM AAVSIAKMIG ARIYTTAGSD AKREMLSRLG VEYVGDSRSV DFADEILELT DGYGVDVVLN SLAGEAIQRG VQILAPGGRF IELGKKDVYA DASLGLAALA KSASFSVVDL DLNLKLQPAR YRQLLQHILQ HVADGKLEVL PVTAFSLHDA ADAFRLMASG KHTGKIVISI PQHGSIEAIA APPPLPLVSR DGGYLIVGGM GGLGFVVARW LAEQGAGLIV LNGRSAPSDE VAAAIAELNA SGSRIEVITG DITEPDTAER LVRAVEDAGF RLAGVVHSAM VLADEIVLNM TDSAARRVFA PKVTGSWRLH VATAARDVDW WLTFSSAAAL LGTPGQGAYA AANSWVDGLV AHRRSAGLPA VGINWGPWAD VGRAQFFKDL GVEMINAEQG LAAMQAVLTA DRGRTGVFSL DARQWFQSFP AVAGSSLFAK LHDSAARKSG QRRGGGAIRA QLDALDAAER PGHLASAIAD EIRAVLRSGD PIDHHRPLET LGLDSLMGLE LRNRLEASLG ITLPVALVWA YPTISDLATA LCERMDYATP AAAQEISDTE PELSDEEMDL LADLVDASEL EAATRGES //