NAPA_DESDA
ID NAPA_DESDA Reviewed; 755 AA.
AC P81186; B8IYC9; Q599G8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Periplasmic nitrate reductase {ECO:0000255|HAMAP-Rule:MF_01630};
DE EC=1.9.6.1 {ECO:0000255|HAMAP-Rule:MF_01630, ECO:0000269|PubMed:16887508, ECO:0000269|PubMed:9367852};
DE Flags: Precursor;
GN Name=napA {ECO:0000255|HAMAP-Rule:MF_01630}; Synonyms=nap;
GN OrderedLocusNames=Ddes_0616;
OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=525146;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN
RP COMPLEX WITH IRON-SULFUR (4FE-4S) AND MOLYBDENUM MOLYBDOPTERIN COFACTOR,
RP AND COFACTOR.
RC STRAIN=ATCC 27774 / DSM 6949 / MB;
RX PubMed=10368307; DOI=10.1016/s0969-2126(99)80010-0;
RA Dias J.M., Than M.E., Humm A., Huber R., Bourenkov G.P., Bartunik H.D.,
RA Bursakov S., Calvete J.J., Caldeira J., Carneiro C., Moura J.J.G.,
RA Moura I., Romao M.J.;
RT "Crystal structure of the first dissimilatory nitrate reductase at 1.9 A
RT solved by MAD methods.";
RL Structure 7:65-79(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15972253; DOI=10.1016/j.femsle.2005.05.042;
RA Marietou A., Richardson D., Cole J., Mohan S.;
RT "Nitrate reduction by Desulfovibrio desulfuricans: a periplasmic nitrate
RT reductase system that lacks NapB, but includes a unique tetraheme c-type
RT cytochrome, NapM.";
RL FEMS Microbiol. Lett. 248:217-225(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27774 / DSM 6949 / MB;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Hazen T.C.;
RT "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT ATCC 27774.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 33-73, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, AND COFACTOR.
RC STRAIN=ATCC 27774 / DSM 6949 / MB;
RX PubMed=9367852; DOI=10.1006/bbrc.1997.7560;
RA Bursakov S.A., Carneiro C., Almendra M.J., Duarte R.O., Caldeira J.,
RA Moura I., Moura J.J.G.;
RT "Enzymatic properties and effect of ionic strength on periplasmic nitrate
RT reductase (NAP) from Desulfovibrio desulfuricans ATCC 27774.";
RL Biochem. Biophys. Res. Commun. 239:816-822(1997).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 27774 / DSM 6949 / MB;
RX PubMed=16887508; DOI=10.1016/s1075-9964(95)80444-7;
RA Bursakov S., Liu M.-Y., Payne W.J., Legall J., Moura I., Moura J.J.G.;
RT "Isolation and preliminary characterization of a soluble nitrate reductase
RT from the sulfate-reducing bacterium Desulfovibrio desulfuricans 27774.";
RL Anaerobe 1:55-60(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 33-755 IN COMPLEX WITH
RP IRON-SULFUR (4FE-4S); MOLYBDENUM MOLYBDOPTERIN COFACTOR AND SUBSTRATE, AND
RP COFACTOR.
RX PubMed=18327621; DOI=10.1007/s00775-008-0359-6;
RA Najmudin S., Gonzalez P.J., Trincao J., Coelho C., Mukhopadhyay A.,
RA Cerqueira N.M., Romao C.C., Moura I., Moura J.J., Brondino C.D.,
RA Romao M.J.;
RT "Periplasmic nitrate reductase revisited: a sulfur atom completes the sixth
RT coordination of the catalytic molybdenum.";
RL J. Biol. Inorg. Chem. 13:737-753(2008).
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:16887508, ECO:0000269|PubMed:9367852}.
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:16887508, ECO:0000269|PubMed:9367852};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:10368307, ECO:0000269|PubMed:16887508,
CC ECO:0000269|PubMed:18327621, ECO:0000269|PubMed:9367852};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:10368307, ECO:0000269|PubMed:16887508,
CC ECO:0000269|PubMed:18327621};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:10368307, ECO:0000269|PubMed:16887508,
CC ECO:0000269|PubMed:18327621, ECO:0000269|PubMed:9367852};
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:10368307, ECO:0000269|PubMed:16887508,
CC ECO:0000269|PubMed:18327621};
CC -!- ACTIVITY REGULATION: Activated by potassium and sodium ions and
CC inhibited by magnesium and calcium ions. {ECO:0000269|PubMed:9367852}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12 uM for nitrate (in the presence of NaCl)
CC {ECO:0000269|PubMed:9367852};
CC KM=20 uM for nitrate {ECO:0000269|PubMed:16887508};
CC KM=32 uM for nitrate (in the absence of NaCl)
CC {ECO:0000269|PubMed:9367852};
CC pH dependence:
CC Optimum pH is between 8 and 9.5. {ECO:0000269|PubMed:16887508,
CC ECO:0000269|PubMed:9367852};
CC -!- SUBUNIT: Monomer (PubMed:16887508). Component of the periplasmic
CC nitrate reductase NapAB complex composed of NapA and NapB (By
CC similarity). {ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:16887508}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:16887508}.
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:9367852). {ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:9367852}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01630, ECO:0000305}.
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DR EMBL; Y18045; CAA77019.1; -; Genomic_DNA.
DR EMBL; AJ920046; CAI72603.1; -; Genomic_DNA.
DR EMBL; CP001358; ACL48525.1; -; Genomic_DNA.
DR PIR; PC4422; PC4422.
DR RefSeq; WP_012624252.1; NC_011883.1.
DR PDB; 2JIM; X-ray; 2.45 A; A=33-755.
DR PDB; 2JIO; X-ray; 2.20 A; A=33-755.
DR PDB; 2JIP; X-ray; 2.30 A; A=33-755.
DR PDB; 2JIQ; X-ray; 2.44 A; A=33-755.
DR PDB; 2JIR; X-ray; 2.35 A; A=33-755.
DR PDB; 2NAP; X-ray; 1.90 A; A=33-755.
DR PDB; 2V3V; X-ray; 1.99 A; A=33-755.
DR PDB; 2V45; X-ray; 2.40 A; A=33-755.
DR PDBsum; 2JIM; -.
DR PDBsum; 2JIO; -.
DR PDBsum; 2JIP; -.
DR PDBsum; 2JIQ; -.
DR PDBsum; 2JIR; -.
DR PDBsum; 2NAP; -.
DR PDBsum; 2V3V; -.
DR PDBsum; 2V45; -.
DR AlphaFoldDB; P81186; -.
DR SMR; P81186; -.
DR STRING; 525146.Ddes_0616; -.
DR PRIDE; P81186; -.
DR EnsemblBacteria; ACL48525; ACL48525; Ddes_0616.
DR KEGG; dds:Ddes_0616; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_4_7; -.
DR OMA; KIVSFWT; -.
DR OrthoDB; 323168at2; -.
DR BRENDA; 1.9.6.1; 1905.
DR EvolutionaryTrace; P81186; -.
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: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 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; IPR010051; Periplasm_NO3_reductase_lsu.
DR InterPro; IPR006311; TAT_signal.
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; SSF50692; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 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; Signal; Transport.
FT SIGNAL 1..32
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:9367852"
FT CHAIN 33..755
FT /note="Periplasmic nitrate reductase"
FT /id="PRO_0000019169"
FT DOMAIN 38..93
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 45
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:10368307, ECO:0000269|PubMed:18327621,
FT ECO:0007744|PDB:2JIM, ECO:0007744|PDB:2JIO,
FT ECO:0007744|PDB:2JIP, ECO:0007744|PDB:2JIQ,
FT ECO:0007744|PDB:2JIR, ECO:0007744|PDB:2NAP,
FT ECO:0007744|PDB:2V3V, ECO:0007744|PDB:2V45"
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:10368307, ECO:0000269|PubMed:18327621,
FT ECO:0007744|PDB:2JIM, ECO:0007744|PDB:2JIO,
FT ECO:0007744|PDB:2JIP, ECO:0007744|PDB:2JIQ,
FT ECO:0007744|PDB:2JIR, ECO:0007744|PDB:2NAP,
FT ECO:0007744|PDB:2V3V, ECO:0007744|PDB:2V45"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:10368307, ECO:0000269|PubMed:18327621,
FT ECO:0007744|PDB:2JIM, ECO:0007744|PDB:2JIO,
FT ECO:0007744|PDB:2JIP, ECO:0007744|PDB:2JIQ,
FT ECO:0007744|PDB:2JIR, ECO:0007744|PDB:2NAP,
FT ECO:0007744|PDB:2V3V, ECO:0007744|PDB:2V45"
FT BINDING 79
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:10368307, ECO:0000269|PubMed:18327621,
FT ECO:0007744|PDB:2JIM, ECO:0007744|PDB:2JIO,
FT ECO:0007744|PDB:2JIP, ECO:0007744|PDB:2JIQ,
FT ECO:0007744|PDB:2JIR, ECO:0007744|PDB:2NAP,
FT ECO:0007744|PDB:2V3V, ECO:0007744|PDB:2V45"
FT BINDING 81
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:10368307, ECO:0000269|PubMed:18327621,
FT ECO:0007744|PDB:2JIM, ECO:0007744|PDB:2JIP,
FT ECO:0007744|PDB:2JIR, ECO:0007744|PDB:2NAP,
FT ECO:0007744|PDB:2V3V, ECO:0007744|PDB:2V45"
FT BINDING 143
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:10368307, ECO:0000269|PubMed:18327621,
FT ECO:0007744|PDB:2JIM, ECO:0007744|PDB:2JIO,
FT ECO:0007744|PDB:2JIP, ECO:0007744|PDB:2JIQ,
FT ECO:0007744|PDB:2JIR, ECO:0007744|PDB:2NAP,
FT ECO:0007744|PDB:2V3V, ECO:0007744|PDB:2V45"
FT BINDING 168
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:10368307, ECO:0000269|PubMed:18327621,
FT ECO:0007744|PDB:2JIM, ECO:0007744|PDB:2JIO,
FT ECO:0007744|PDB:2JIP, ECO:0007744|PDB:2JIQ,
FT ECO:0007744|PDB:2JIR, ECO:0007744|PDB:2NAP,
FT ECO:0007744|PDB:2V3V, ECO:0007744|PDB:2V45"
FT BINDING 172
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:10368307, ECO:0000269|PubMed:18327621,
FT ECO:0007744|PDB:2JIM, ECO:0007744|PDB:2JIO,
FT ECO:0007744|PDB:2JIP, ECO:0007744|PDB:2JIQ,
FT ECO:0007744|PDB:2JIR, ECO:0007744|PDB:2NAP,
FT ECO:0007744|PDB:2V3V, ECO:0007744|PDB:2V45"
FT BINDING 208..212
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:10368307,
FT ECO:0000269|PubMed:18327621, ECO:0007744|PDB:2JIM,
FT ECO:0007744|PDB:2JIO, ECO:0007744|PDB:2JIP,
FT ECO:0007744|PDB:2JIQ, ECO:0007744|PDB:2JIR,
FT ECO:0007744|PDB:2NAP, ECO:0007744|PDB:2V3V,
FT ECO:0007744|PDB:2V45"
FT BINDING 236..238
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:10368307,
FT ECO:0000269|PubMed:18327621, ECO:0007744|PDB:2JIM,
FT ECO:0007744|PDB:2JIO, ECO:0007744|PDB:2JIP,
FT ECO:0007744|PDB:2JIQ, ECO:0007744|PDB:2JIR,
FT ECO:0007744|PDB:2NAP, ECO:0007744|PDB:2V3V,
FT ECO:0007744|PDB:2V45"
FT BINDING 255..257
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:10368307, ECO:0000269|PubMed:18327621,
FT ECO:0007744|PDB:2JIM, ECO:0007744|PDB:2JIO,
FT ECO:0007744|PDB:2JIP, ECO:0007744|PDB:2JIQ,
FT ECO:0007744|PDB:2JIR, ECO:0007744|PDB:2NAP,
FT ECO:0007744|PDB:2V3V, ECO:0007744|PDB:2V45"
FT BINDING 340
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:10368307, ECO:0000269|PubMed:18327621,
FT ECO:0007744|PDB:2JIM, ECO:0007744|PDB:2JIO,
FT ECO:0007744|PDB:2JIP, ECO:0007744|PDB:2JIQ,
FT ECO:0007744|PDB:2JIR, ECO:0007744|PDB:2NAP,
FT ECO:0007744|PDB:2V3V, ECO:0007744|PDB:2V45"
FT BINDING 344
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:10368307, ECO:0000269|PubMed:18327621,
FT ECO:0007744|PDB:2JIM, ECO:0007744|PDB:2JIP,
FT ECO:0007744|PDB:2JIQ, ECO:0007744|PDB:2JIR,
FT ECO:0007744|PDB:2NAP, ECO:0007744|PDB:2V3V,
FT ECO:0007744|PDB:2V45"
FT BINDING 450
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:10368307, ECO:0000269|PubMed:18327621,
FT ECO:0007744|PDB:2JIM, ECO:0007744|PDB:2JIO,
FT ECO:0007744|PDB:2JIP, ECO:0007744|PDB:2JIQ,
FT ECO:0007744|PDB:2JIR, ECO:0007744|PDB:2NAP,
FT ECO:0007744|PDB:2V3V, ECO:0007744|PDB:2V45"
FT BINDING 475..477
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:10368307,
FT ECO:0000269|PubMed:18327621, ECO:0007744|PDB:2JIM,
FT ECO:0007744|PDB:2JIO, ECO:0007744|PDB:2JIP,
FT ECO:0007744|PDB:2JIQ, ECO:0007744|PDB:2JIR,
FT ECO:0007744|PDB:2NAP, ECO:0007744|PDB:2V3V,
FT ECO:0007744|PDB:2V45"
FT BINDING 647..656
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:10368307, ECO:0000269|PubMed:18327621,
FT ECO:0007744|PDB:2JIM, ECO:0007744|PDB:2JIO,
FT ECO:0007744|PDB:2JIP, ECO:0007744|PDB:2JIQ,
FT ECO:0007744|PDB:2JIR, ECO:0007744|PDB:2NAP,
FT ECO:0007744|PDB:2V3V, ECO:0007744|PDB:2V45"
FT BINDING 648..653
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:18327621,
FT ECO:0007744|PDB:2JIQ, ECO:0007744|PDB:2JIR"
FT BINDING 721
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000305|PubMed:18327621, ECO:0007744|PDB:2JIQ,
FT ECO:0007744|PDB:2JIR"
FT BINDING 729
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:10368307, ECO:0000269|PubMed:18327621,
FT ECO:0007744|PDB:2JIM, ECO:0007744|PDB:2JIO,
FT ECO:0007744|PDB:2JIP, ECO:0007744|PDB:2JIQ,
FT ECO:0007744|PDB:2JIR, ECO:0007744|PDB:2NAP,
FT ECO:0007744|PDB:2V3V, ECO:0007744|PDB:2V45"
FT BINDING 746
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:10368307, ECO:0000269|PubMed:18327621,
FT ECO:0007744|PDB:2JIM, ECO:0007744|PDB:2JIO,
FT ECO:0007744|PDB:2JIP, ECO:0007744|PDB:2JIQ,
FT ECO:0007744|PDB:2JIR, ECO:0007744|PDB:2NAP,
FT ECO:0007744|PDB:2V3V, ECO:0007744|PDB:2V45"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:2NAP"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:2V3V"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2V3V"
FT HELIX 113..131
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:2NAP"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:2NAP"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 257..270
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 276..282
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 307..314
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 318..330
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 331..338
FT /evidence="ECO:0007829|PDB:2NAP"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 348..362
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:2V3V"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:2NAP"
FT TURN 385..389
FT /evidence="ECO:0007829|PDB:2NAP"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 404..414
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 429..438
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 443..448
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 451..454
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 458..465
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 471..475
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 482..485
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 488..491
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 501..504
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 508..513
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 526..537
FT /evidence="ECO:0007829|PDB:2NAP"
FT TURN 541..544
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 549..560
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 572..577
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:2NAP"
FT TURN 599..601
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 610..613
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 623..626
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 639..641
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 643..648
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 657..659
FT /evidence="ECO:0007829|PDB:2JIO"
FT HELIX 660..662
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 664..667
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 675..678
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 679..685
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 692..697
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 700..712
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 716..720
FT /evidence="ECO:0007829|PDB:2NAP"
FT HELIX 728..730
FT /evidence="ECO:0007829|PDB:2NAP"
FT TURN 738..740
FT /evidence="ECO:0007829|PDB:2NAP"
FT STRAND 748..754
FT /evidence="ECO:0007829|PDB:2NAP"
SQ SEQUENCE 755 AA; 83497 MW; D54BDB9D1FE21DC2 CRC64;
MSTSRRDFLK YFAMSAAVAA ASGAGFGSLA LAADNRPEKW VKGVCRYCGT GCGVLVGVKD
GKAVAIQGDP NNHNAGLLCL KGSLLIPVLN SKERVTQPLV RRHKGGKLEP VSWDEALDLM
ASRFRSSIDM YGPNSVAWYG SGQCLTEESY VANKIFKGGF GTNNVDGNPR LCMASAVGGY
VTSFGKDEPM GTYADIDQAT CFFIIGSNTS EAHPVLFRRI ARRKQVEPGV KIIVADPRRT
NTSRIADMHV AFRPGTDLAF MHSMAWVIIN EELDNPRFWQ RYVNFMDAEG KPSDFEGYKA
FLENYRPEKV AEICRVPVEQ IYGAARAFAE SAATMSLWCM GINQRVQGVF ANNLIHNLHL
ITGQICRPGA TSFSLTGQPN ACGGVRDGGA LSHLLPAGRA IPNAKHRAEM EKLWGLPEGR
IAPEPGYHTV ALFEALGRGD VKCMIICETN PAHTLPNLNK VHKAMSHPES FIVCIEAFPD
AVTLEYADLV LPPAFWCERD GVYGCGERRY SLTEKAVDPP GQCRPTVNTL VEFARRAGVD
PQLVNFRNAE DVWNEWRMVS KGTTYDFWGM TRERLRKESG LIWPCPSEDH PGTSLRYVRG
QDPCVPADHP DRFFFYGKPD GRAVIWMRPA KGAAEEPDAE YPLYLTSMRV IDHWHTATMT
GKVPELQKAN PIAFVEINEE DAARTGIKHG DSVIVETRRD AMELPARVSD VCRPGLIAVP
FFDPKKLVNK LFLDATDPVS REPEYKICAA RVRKA
