ID   NAPA_CUPNH              Reviewed;         831 AA.
AC   P39185; Q7WXC3;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   27-MAR-2024, entry version 173.
DE   RecName: Full=Periplasmic nitrate reductase {ECO:0000255|HAMAP-Rule:MF_01630};
DE            EC=1.9.6.1 {ECO:0000255|HAMAP-Rule:MF_01630};
DE   Flags: Precursor;
GN   Name=napA {ECO:0000255|HAMAP-Rule:MF_01630,
GN   ECO:0000303|PubMed:8376334}; OrderedLocusNames=PHG211;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OG   Plasmid megaplasmid pHG1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-50, FUNCTION,
RP   CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier
RC   337;
RX   PubMed=8376334; DOI=10.1128/jb.175.18.5867-5876.1993;
RA   Siddiqui R.A., Warnecke-Eberz U., Hengsberger A., Schneider B., Kostka S.,
RA   Friedrich B.;
RT   "Structure and function of a periplasmic nitrate reductase in Alcaligenes
RT   eutrophus H16.";
RL   J. Bacteriol. 175:5867-5876(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier
RC   337;
RX   PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA   Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT   "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT   encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL   J. Mol. Biol. 332:369-383(2003).
RN   [3] {ECO:0007744|PDB:3ML1, ECO:0007744|PDB:3O5A}
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 30-831 IN COMPLEX WITH
RP   IRON-SULFUR (4FE-4S) AND MOLYBDENUM MOLYBDOPTERIN COFACTOR, COFACTOR, AND
RP   SUBUNIT.
RX   PubMed=21419779; DOI=10.1016/j.jmb.2011.03.016;
RA   Coelho C., Gonzalez P.J., Moura J.G., Moura I., Trincao J., Joao Romao M.;
RT   "The crystal structure of Cupriavidus necator nitrate reductase in oxidized
RT   and partially reduced states.";
RL   J. Mol. Biol. 408:932-948(2011).
CC   -!- FUNCTION: Catalytic subunit of the periplasmic nitrate reductase
CC       complex NapAB. Receives electrons from NapB and catalyzes the reduction
CC       of nitrate to nitrite. {ECO:0000255|HAMAP-Rule:MF_01630,
CC       ECO:0000269|PubMed:8376334}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(II)-[cytochrome] + 2 H(+) + nitrate = 2 Fe(III)-
CC         [cytochrome] + H2O + nitrite; Xref=Rhea:RHEA:12909, Rhea:RHEA-
CC         COMP:11777, Rhea:RHEA-COMP:11778, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632,
CC         ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.9.6.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01630,
CC         ECO:0000269|PubMed:8376334};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01630,
CC         ECO:0000269|PubMed:21419779};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01630,
CC       ECO:0000269|PubMed:21419779};
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000255|HAMAP-Rule:MF_01630,
CC         ECO:0000269|PubMed:21419779};
CC       Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC       bis-MGD) cofactor per subunit. {ECO:0000255|HAMAP-Rule:MF_01630,
CC       ECO:0000269|PubMed:21419779};
CC   -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB complex
CC       composed of NapA and NapB. {ECO:0000255|HAMAP-Rule:MF_01630,
CC       ECO:0000269|PubMed:21419779, ECO:0000269|PubMed:8376334}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01630,
CC       ECO:0000305|PubMed:8376334}.
CC   -!- INDUCTION: Expressed independently of nitrate induction and
CC       anaerobiosis.
CC   -!- PTM: Predicted to be exported by the Tat system (By similarity). The
CC       position of the signal peptide cleavage has been experimentally proven
CC       (PubMed:8376334). {ECO:0000255|HAMAP-Rule:MF_01630,
CC       ECO:0000269|PubMed:8376334}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. NasA/NapA/NarB subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01630}.
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DR   EMBL; X71385; CAA50507.1; -; Genomic_DNA.
DR   EMBL; AY305378; AAP85963.1; -; Genomic_DNA.
DR   PIR; A48489; A48489.
DR   RefSeq; WP_011154126.1; NZ_CP039289.1.
DR   PDB; 3ML1; X-ray; 1.60 A; A=30-831.
DR   PDB; 3O5A; X-ray; 1.72 A; A=30-831.
DR   PDBsum; 3ML1; -.
DR   PDBsum; 3O5A; -.
DR   AlphaFoldDB; P39185; -.
DR   SMR; P39185; -.
DR   GeneID; 39976666; -.
DR   KEGG; reh:PHG211; -.
DR   PATRIC; fig|381666.6.peg.159; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_4_4; -.
DR   OrthoDB; 7376058at2; -.
DR   BRENDA; 1.9.6.1; 231.
DR   Proteomes; UP000008210; Plasmid megaplasmid pHG1.
DR   GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0050140; F:nitrate reductase (cytochrome) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniRule.
DR   CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 1.
DR   CDD; cd02754; MopB_Nitrate-R-NapA-like; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.30.200.210; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   HAMAP; MF_01630; Nitrate_reduct_NapA; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR041957; CT_Nitrate-R-NapA-like.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   InterPro; IPR010051; Periplasm_NO3_reductase_lsu.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   NCBIfam; TIGR01706; NAPA; 1.
DR   NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR   PANTHER; PTHR43105:SF11; PERIPLASMIC NITRATE REDUCTASE; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Molybdenum; Nitrate assimilation;
KW   Oxidoreductase; Periplasm; Plasmid; Reference proteome; Signal; Transport.
FT   SIGNAL          1..29
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:8376334"
FT   CHAIN           30..831
FT                   /note="Periplasmic nitrate reductase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT                   /id="PRO_0000019168"
FT   DOMAIN          41..97
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         48
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   BINDING         51
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   BINDING         55
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   BINDING         83
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   BINDING         85
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   BINDING         152
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   BINDING         177
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   BINDING         181
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   BINDING         214..221
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   BINDING         245..249
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   BINDING         264..266
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   BINDING         375
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   BINDING         379
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   BINDING         485
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   BINDING         511..512
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   BINDING         534
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   BINDING         561
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   BINDING         721..730
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   BINDING         797
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT   BINDING         805
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   BINDING         822
FT                   /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT                   /ligand_id="ChEBI:CHEBI:60539"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT                   ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT                   ECO:0007744|PDB:3O5A"
FT   CONFLICT        146..151
FT                   /note="GMFGSG -> ACSAPA (in Ref. 1; CAA50507)"
FT                   /evidence="ECO:0000305"
FT   STRAND          40..47
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          56..62
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          65..71
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   TURN            76..80
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           84..87
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           88..91
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          103..107
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          115..119
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           122..139
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           142..144
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          145..149
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           155..166
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   TURN            167..169
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          174..176
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           177..180
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           183..193
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           202..206
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          209..215
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           218..221
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           223..235
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          240..248
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           250..253
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          256..260
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   TURN            263..265
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           266..279
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           285..291
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          292..297
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           310..314
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          324..327
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           329..337
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           341..348
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           352..363
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          369..374
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           375..378
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           383..397
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          405..409
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   TURN            414..419
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           420..423
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           439..448
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           464..472
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          478..483
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           486..489
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   TURN            493..496
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           497..502
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          507..514
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           517..520
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          523..529
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           531..533
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          536..539
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          543..548
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           561..569
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           574..577
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           580..583
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           587..589
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           594..598
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          600..603
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           609..611
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           619..624
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           628..640
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   TURN            641..644
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           650..655
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          659..662
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          670..674
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   TURN            675..677
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          697..701
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          713..715
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          717..722
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           734..736
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           738..743
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          748..751
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           753..758
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          766..770
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          775..785
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          792..797
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   HELIX           804..806
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   TURN            814..816
FT                   /evidence="ECO:0007829|PDB:3ML1"
FT   STRAND          824..830
FT                   /evidence="ECO:0007829|PDB:3ML1"
SQ   SEQUENCE   831 AA;  93346 MW;  34CE1CDE6677C42F CRC64;
     MKISRRDFIK QTAITATASV AGVTLPAGAA NFVTDSEVTK LKWSKAPCRF CGTGCGVTVA
     VKDNKVVATQ GDPQAEVNKG LNCVKGYFLS KIMYGQDRLT RPLMRMKNGK YDKNGDFAPV
     TWDQAFDEME RQFKRVLKEK GPTAVGMFGS GQWTVWEGYA AAKLYKAGFR SNNIDPNARH
     CMASAAAGFM RTFGMDEPMG CYDDFEAADA FVLWGSNMAE MHPILWTRVT DRRLSHPKTR
     VVVLSTFTHR CFDLADIGII FKPQTDLAML NYIANYIIRN NKVNKDFVNK HTVFKEGVTD
     IGYGLRPDHP LQKAAKNASD PGAAKVITFD EFAKFVSKYD ADYVSKLSAV PKAKLDQLAE
     LYADPNIKVM SLWTMGFNQH TRGTWANNMV YNLHLLTGKI ATPGNSPFSL TGQPSACGTA
     REVGTFSHRL PADMVVTNPK HREEAERIWK LPPGTIPDKP GYDAVLQNRM LKDGKLNAYW
     VQVNNNMQAA ANLMEEGLPG YRNPANFIVV SDAYPTVTAL AADLVLPSAM WVEKEGAYGN
     AERRTQFWHQ LVDAPGEARS DLWQLVEFAK RFKVEEVWPP ELIAKKPEYK GKTLYDVLYR
     NGQVDKFPLK DVNAEYHNAE AKAFGFYLQK GLFEEYATFG RGHGHDLAPF DAYHEARGLR
     WPVVNGKETR WRYREGSDPY VKAGTGFQFY GNPDGKAVIF ALPYEPPAES PDKEYPYWLV
     TGRVLEHWHS GSMTRRVPEL YRSFPNAVVF MHPEDAKALG LRRGVEVEVV SRRGRMRSRI
     ETRGRDAPPR GLVFVPWFDA SQLINKVTLD ATCPISLQTD FKKCAVKIVK V
//