ID NARH_ECOLI Reviewed; 512 AA. AC P11349; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 3. DT 27-MAR-2024, entry version 208. DE RecName: Full=Respiratory nitrate reductase 1 beta chain; DE EC=1.7.5.1; DE AltName: Full=Nitrate reductase A subunit beta; DE AltName: Full=Quinol-nitrate oxidoreductase subunit beta; GN Name=narH; OrderedLocusNames=b1225, JW1216; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12 / TG1; RX PubMed=2674654; DOI=10.1007/bf00331275; RA Blasco F., Iobbi C., Giordano G., Chippaux M., Bonnefoy V.; RT "Nitrate reductase of Escherichia coli: completion of the nucleotide RT sequence of the nar operon and reassessment of the role of the alpha and RT beta subunits in iron binding and electron transfer."; RL Mol. Gen. Genet. 218:249-256(1989). RN [2] RP SEQUENCE REVISION TO 398-417. RC STRAIN=K12 / TG1; RA Blasco F.; RL Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8905232; DOI=10.1093/dnares/3.3.137; RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., RA Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 12.7-28.0 min region on the linkage map."; RL DNA Res. 3:137-155(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 365-512. RX PubMed=2832376; DOI=10.1128/jb.170.4.1721-1729.1988; RA Sodergren E.J., Demoss J.A.; RT "narI region of the Escherichia coli nitrate reductase (nar) operon RT contains two genes."; RL J. Bacteriol. 170:1721-1729(1988). RN [7] RP PROTEIN SEQUENCE OF 1-10. RX PubMed=3053688; DOI=10.1016/s0021-9258(18)37572-0; RA Sodergren E.J., Hsu P.Y., Demoss J.A.; RT "Roles of the narJ and narI gene products in the expression of nitrate RT reductase in Escherichia coli."; RL J. Biol. Chem. 263:16156-16162(1988). RN [8] RP EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS. RX PubMed=1321049; DOI=10.1111/j.1432-1033.1992.tb17020.x; RA Guigliarelli B., Asso M., More C., Augier V., Blasco F., Pommier J., RA Giordano G., Bertrand P.; RT "EPR and redox characterization of iron-sulfur centers in nitrate RT reductases A and Z from Escherichia coli. Evidence for a high-potential and RT a low-potential class and their relevance in the electron-transfer RT mechanism."; RL Eur. J. Biochem. 207:61-68(1992). RN [9] RP MUTAGENESIS OF CYSTEINE RESIDUES, AND EPR SPECTROSCOPY OF IRON-SULFUR RP CLUSTERS. RX PubMed=8383531; DOI=10.1021/bi00059a018; RA Augier V., Guigliarelli B., Asso M., Bertrand P., Frixon C., Giordano G., RA Chippaux M., Blasco F.; RT "Site-directed mutagenesis of conserved cysteine residues within the beta RT subunit of Escherichia coli nitrate reductase. Physiological, biochemical, RT and EPR characterization of the mutated enzymes."; RL Biochemistry 32:2013-2023(1993). RN [10] RP MUTAGENESIS OF CYSTEINE RESIDUES, AND EPR SPECTROSCOPY OF IRON-SULFUR RP CLUSTERS. RX PubMed=8388253; DOI=10.1021/bi00070a018; RA Augier V., Asso M., Guigliarelli B., More C., Bertrand P., Santini C.-L., RA Blasco F., Chippaux M., Giordano G.; RT "Removal of the high-potential [4Fe-4S] center of the beta-subunit from RT Escherichia coli nitrate reductase. Physiological, biochemical, and EPR RT characterization of site-directed mutated enzymes."; RL Biochemistry 32:5099-5108(1993). RN [11] RP MUTAGENESIS OF CYSTEINE RESIDUES, AND EPR SPECTROSCOPY OF IRON-SULFUR RP CLUSTERS. RX PubMed=8664273; DOI=10.1021/bi952459p; RA Guigliarelli B., Magalon A., Asso M., Bertrand P., Frixon C., Giordano G., RA Blasco F.; RT "Complete coordination of the four Fe-S centers of the beta subunit from RT Escherichia coli nitrate reductase. Physiological, biochemical, and EPR RT characterization of site-directed mutants lacking the highest or lowest RT potential [4Fe-4S] clusters."; RL Biochemistry 35:4828-4836(1996). RN [12] RP EPR SPECTROSCOPY, AND REDOX POTENTIOMETRY OF IRON-SULFUR CLUSTERS. RX PubMed=9516445; DOI=10.1074/jbc.273.13.7462; RA Rothery R.A., Magalon A., Giordano G., Guigliarelli B., Blasco F., RA Weiner J.H.; RT "The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI). RT Effect of a mobAB mutation and interactions with [Fe-S] clusters."; RL J. Biol. Chem. 273:7462-7469(1998). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (3FE-4S) RP AND IRON-SULFUR (4FE-4S), COFACTOR, AND SUBUNIT. RX PubMed=12910261; DOI=10.1038/nsb969; RA Bertero M.G., Rothery R.A., Palak M., Hou C., Lim D., Blasco F., RA Weiner J.H., Strynadka N.C.J.; RT "Insights into the respiratory electron transfer pathway from the structure RT of nitrate reductase A."; RL Nat. Struct. Biol. 10:681-687(2003). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (3FE-4S) RP AND IRON-SULFUR (4FE-4S), AND COFACTOR. RX PubMed=14725769; DOI=10.1016/j.str.2003.11.020; RA Jormakka M., Richardson D., Byrne B., Iwata S.; RT "Architecture of NarGH reveals a structural classification of Mo-bisMGD RT enzymes."; RL Structure 12:95-104(2004). CC -!- FUNCTION: The nitrate reductase enzyme complex allows E.coli to use CC nitrate as an electron acceptor during anaerobic growth. The beta chain CC is an electron transfer unit containing four cysteine clusters involved CC in the formation of iron-sulfur centers. Electrons are transferred from CC the gamma chain to the molybdenum cofactor of the alpha subunit. CC -!- CATALYTIC ACTIVITY: CC Reaction=a quinol + nitrate = a quinone + H2O + nitrite; CC Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301, CC ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.7.5.1; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000269|PubMed:12910261, ECO:0000269|PubMed:14725769}; CC Note=Binds 3 [4Fe-4S] clusters per subunit. CC {ECO:0000269|PubMed:12910261, ECO:0000269|PubMed:14725769}; CC -!- COFACTOR: CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; CC Evidence={ECO:0000269|PubMed:12910261, ECO:0000269|PubMed:14725769}; CC Note=Binds 1 [3Fe-4S] cluster per subunit. CC {ECO:0000269|PubMed:12910261, ECO:0000269|PubMed:14725769}; CC -!- SUBUNIT: Dimer of heterotrimers each composed of an alpha, a beta and a CC gamma chain. Alpha and beta are catalytic chains; gamma chains are CC involved in binding the enzyme complex to the cytoplasmic membrane. CC {ECO:0000269|PubMed:12910261}. CC -!- INTERACTION: CC P11349; P42593: fadH; NbExp=3; IntAct=EBI-555067, EBI-561933; CC P11349; P09152: narG; NbExp=13; IntAct=EBI-555067, EBI-547248; CC P11349; P19317: narW; NbExp=3; IntAct=EBI-555067, EBI-555088; CC P11349; P19318: narY; NbExp=3; IntAct=EBI-555067, EBI-555059; CC P11349; P19319: narZ; NbExp=6; IntAct=EBI-555067, EBI-547262; CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. CC -!- INDUCTION: By nitrate. CC -!- WEB RESOURCE: Name=Worthington enzyme manual; CC URL="https://www.worthington-biochem.com/NAR/"; 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; M20147; AAA24195.1; -; Genomic_DNA. DR EMBL; U00096; AAC74309.1; -; Genomic_DNA. DR EMBL; AP009048; BAA36095.1; -; Genomic_DNA. DR EMBL; X16181; CAA34304.1; -; Genomic_DNA. DR PIR; F64869; RDECNB. DR RefSeq; NP_415743.1; NC_000913.3. DR RefSeq; WP_000702650.1; NZ_STEB01000023.1. DR PDB; 1Q16; X-ray; 1.90 A; B=1-512. DR PDB; 1R27; X-ray; 2.00 A; B/D=1-512. DR PDB; 1SIW; X-ray; 2.20 A; B=1-512. DR PDB; 1Y4Z; X-ray; 2.00 A; B=1-512. DR PDB; 1Y5I; X-ray; 1.90 A; B=1-512. DR PDB; 1Y5L; X-ray; 2.50 A; B=1-512. DR PDB; 1Y5N; X-ray; 2.50 A; B=1-512. DR PDB; 3EGW; X-ray; 1.90 A; B=1-509. DR PDB; 3IR5; X-ray; 2.30 A; B=1-512. DR PDB; 3IR6; X-ray; 2.80 A; B=1-512. DR PDB; 3IR7; X-ray; 2.50 A; B=1-512. DR PDBsum; 1Q16; -. DR PDBsum; 1R27; -. DR PDBsum; 1SIW; -. DR PDBsum; 1Y4Z; -. DR PDBsum; 1Y5I; -. DR PDBsum; 1Y5L; -. DR PDBsum; 1Y5N; -. DR PDBsum; 3EGW; -. DR PDBsum; 3IR5; -. DR PDBsum; 3IR6; -. DR PDBsum; 3IR7; -. DR AlphaFoldDB; P11349; -. DR SMR; P11349; -. DR BioGRID; 4262231; 28. DR BioGRID; 850147; 6. DR ComplexPortal; CPX-1974; Nitrate reductase A complex. DR DIP; DIP-10312N; -. DR IntAct; P11349; 15. DR STRING; 511145.b1225; -. DR DrugBank; DB07349; (1S)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PENTANOYLOXY)METHYL]ETHYL OCTANOATE. DR DrugBank; DB04464; N-Formylmethionine. DR TCDB; 5.A.3.1.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family. DR jPOST; P11349; -. DR PaxDb; 511145-b1225; -. DR EnsemblBacteria; AAC74309; AAC74309; b1225. DR GeneID; 75057227; -. DR GeneID; 945780; -. DR KEGG; ecj:JW1216; -. DR KEGG; eco:b1225; -. DR PATRIC; fig|1411691.4.peg.1056; -. DR EchoBASE; EB0633; -. DR eggNOG; COG1140; Bacteria. DR HOGENOM; CLU_043374_5_2_6; -. DR InParanoid; P11349; -. DR OMA; KVYFNWQ; -. DR OrthoDB; 9779457at2; -. DR PhylomeDB; P11349; -. DR BioCyc; EcoCyc:NARH-MONOMER; -. DR BioCyc; MetaCyc:NARH-MONOMER; -. DR BRENDA; 1.7.5.1; 2026. DR EvolutionaryTrace; P11349; -. DR PHI-base; PHI:10513; -. DR PRO; PR:P11349; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0016020; C:membrane; IDA:ComplexPortal. DR GO; GO:0044799; C:NarGHI complex; IDA:EcoCyc. DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IDA:EcoCyc. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc. DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008940; F:nitrate reductase activity; IMP:EcoCyc. DR GO; GO:0019645; P:anaerobic electron transport chain; IDA:ComplexPortal. DR GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc. DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW. DR GO; GO:0042126; P:nitrate metabolic process; IDA:ComplexPortal. DR CDD; cd10557; NarH_beta-like; 1. DR Gene3D; 3.30.70.20; -; 3. DR Gene3D; 1.10.3650.10; nitrate reductase domain like; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR029263; Nitr_red_bet_C. DR InterPro; IPR038262; Nitr_red_bet_C_sf. DR InterPro; IPR006547; NO3_Rdtase_bsu. DR NCBIfam; TIGR01660; narH; 1. DR PANTHER; PTHR43518; NITRATE REDUCTASE BETA SUBUNIT; 1. DR PANTHER; PTHR43518:SF1; RESPIRATORY NITRATE REDUCTASE 1 BETA CHAIN; 1. DR Pfam; PF13247; Fer4_11; 1. DR Pfam; PF14711; Nitr_red_bet_C; 1. DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 3. PE 1: Evidence at protein level; KW 3D-structure; 3Fe-4S; 4Fe-4S; Cell membrane; Direct protein sequencing; KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding; KW Nitrate assimilation; Oxidoreductase; Reference proteome; Repeat; KW Transport. FT CHAIN 1..512 FT /note="Respiratory nitrate reductase 1 beta chain" FT /id="PRO_0000096720" FT DOMAIN 7..35 FT /note="4Fe-4S ferredoxin-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT DOMAIN 175..206 FT /note="4Fe-4S ferredoxin-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT DOMAIN 208..237 FT /note="4Fe-4S ferredoxin-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 16 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:12910261, FT ECO:0000269|PubMed:14725769" FT BINDING 19 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:12910261, FT ECO:0000269|PubMed:14725769" FT BINDING 22 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:12910261, FT ECO:0000269|PubMed:14725769" FT BINDING 26 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:12910261, FT ECO:0000269|PubMed:14725769" FT BINDING 184 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:12910261, FT ECO:0000269|PubMed:14725769" FT BINDING 187 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:12910261, FT ECO:0000269|PubMed:14725769" FT BINDING 192 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:12910261, FT ECO:0000269|PubMed:14725769" FT BINDING 196 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000269|PubMed:12910261, FT ECO:0000269|PubMed:14725769" FT BINDING 217 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000269|PubMed:12910261, FT ECO:0000269|PubMed:14725769" FT BINDING 223 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000269|PubMed:12910261, FT ECO:0000269|PubMed:14725769" FT BINDING 227 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:12910261, FT ECO:0000269|PubMed:14725769" FT BINDING 244 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:12910261, FT ECO:0000269|PubMed:14725769" FT BINDING 247 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:12910261, FT ECO:0000269|PubMed:14725769" FT BINDING 259 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:12910261, FT ECO:0000269|PubMed:14725769" FT BINDING 263 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:12910261, FT ECO:0000269|PubMed:14725769" FT CONFLICT 398..417 FT /note="DTKPVLRALKRMLAMRHYKR -> EYQTGTARTETYAGDASLQT (in FT Ref. 6; AAA24195)" FT /evidence="ECO:0000305" FT STRAND 3..12 FT /evidence="ECO:0007829|PDB:1Q16" FT TURN 13..15 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 21..30 FT /evidence="ECO:0007829|PDB:1Q16" FT STRAND 41..49 FT /evidence="ECO:0007829|PDB:1Q16" FT TURN 51..57 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 59..62 FT /evidence="ECO:0007829|PDB:1Q16" FT STRAND 65..68 FT /evidence="ECO:0007829|PDB:1Q16" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 81..85 FT /evidence="ECO:0007829|PDB:1Q16" FT TURN 86..89 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 97..100 FT /evidence="ECO:0007829|PDB:1Q16" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 109..113 FT /evidence="ECO:0007829|PDB:1Q16" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:1Q16" FT TURN 129..131 FT /evidence="ECO:0007829|PDB:1Q16" FT TURN 142..148 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 152..155 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 159..161 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 167..170 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 172..174 FT /evidence="ECO:0007829|PDB:1Q16" FT STRAND 178..182 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 191..194 FT /evidence="ECO:0007829|PDB:1Q16" FT STRAND 201..204 FT /evidence="ECO:0007829|PDB:1Q16" FT TURN 205..207 FT /evidence="ECO:0007829|PDB:1Q16" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:1Q16" FT TURN 214..216 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 223..226 FT /evidence="ECO:0007829|PDB:1Q16" FT STRAND 232..235 FT /evidence="ECO:0007829|PDB:1Q16" FT TURN 236..239 FT /evidence="ECO:0007829|PDB:1Q16" FT STRAND 240..243 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 248..251 FT /evidence="ECO:0007829|PDB:1Q16" FT TURN 252..254 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 258..261 FT /evidence="ECO:0007829|PDB:1Q16" FT STRAND 268..276 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 277..279 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 280..284 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 289..291 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 292..297 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 306..314 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 319..325 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 329..334 FT /evidence="ECO:0007829|PDB:1Q16" FT STRAND 341..343 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 345..347 FT /evidence="ECO:0007829|PDB:1Q16" FT STRAND 352..356 FT /evidence="ECO:0007829|PDB:1Q16" FT STRAND 366..368 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 380..382 FT /evidence="ECO:0007829|PDB:1Q16" FT STRAND 383..385 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 387..394 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 399..420 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 428..432 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 437..447 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 452..455 FT /evidence="ECO:0007829|PDB:1Q16" FT TURN 463..466 FT /evidence="ECO:0007829|PDB:1Q16" FT HELIX 469..475 FT /evidence="ECO:0007829|PDB:1Q16" SQ SEQUENCE 512 AA; 58066 MW; 2E7719C8D078BAEA CRC64; MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TSREGVEYAW FNNVETKPGQ GFPTDWENQE KYKGGWIRKI NGKLQPRMGN RAMLLGKIFA NPHLPGIDDY YEPFDFDYQN LHTAPEGSKS QPIARPRSLI TGERMAKIEK GPNWEDDLGG EFDKLAKDKN FDNIQKAMYS QFENTFMMYL PRLCEHCLNP ACVATCPSGA IYKREEDGIV LIDQDKCRGW RMCITGCPYK KIYFNWKSGK SEKCIFCYPR IEAGQPTVCS ETCVGRIRYL GVLLYDADAI ERAASTENEK DLYQRQLDVF LDPNDPKVIE QAIKDGIPLS VIEAAQQSPV YKMAMEWKLA LPLHPEYRTL PMVWYVPPLS PIQSAADAGE LGSNGILPDV ESLRIPVQYL ANLLTAGDTK PVLRALKRML AMRHYKRAET VDGKVDTRAL EEVGLTEAQA QEMYRYLAIA NYEDRFVVPS SHRELAREAF PEKNGCGFTF GDGCHGSDTK FNLFNSRRID AIDVTSKTEP HP //