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Database: UniProt
Entry: G2DB50_9GAMM
LinkDB: G2DB50_9GAMM
Original site: G2DB50_9GAMM 
ID   G2DB50_9GAMM            Unreviewed;       179 AA.
AC   G2DB50;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Periplasmic nitrate reductase {ECO:0000313|EMBL:EGV52158.1};
DE            EC=1.7.99.4 {ECO:0000313|EMBL:EGV52158.1};
GN   Name=napA' {ECO:0000313|EMBL:EGV52158.1};
GN   ORFNames=Rifp1Sym_ao00240 {ECO:0000313|EMBL:EGV52158.1};
OS   endosymbiont of Riftia pachyptila (vent Ph05).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=1048808 {ECO:0000313|EMBL:EGV52158.1, ECO:0000313|Proteomes:UP000004491};
RN   [1] {ECO:0000313|EMBL:EGV52158.1, ECO:0000313|Proteomes:UP000004491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA   Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA   Sievert S.M., Schweder T.;
RT   "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT   jerichonana share an identical physiology as revealed by proteogenomic
RT   analyses.";
RL   ISME J. 0:0-0(2011).
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGV52158.1}.
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DR   EMBL; AFOC01000015; EGV52158.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2DB50; -.
DR   PATRIC; fig|1048808.3.peg.805; -.
DR   Proteomes; UP000004491; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
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   SMART; SM00926; Molybdop_Fe4S4; 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   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW   Oxidoreductase {ECO:0000313|EMBL:EGV52158.1};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          40..96
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   179 AA;  19266 MW;  290529BE692655C0 CRC64;
     MKLTRRDFIK SNAVAAAASV AGVTLPAIKT ATAAEGDDGI RWDKAACRYC GTGCSVLMGV
     KDGKVVASQG DPDAPVNKGL NCIKGYFLPK ILYGKDRLTT PMLRKKNGKY DKNGKFEAVS
     WDEAFKTMAE KWVAARKAKG PKGVGMFGSG QWTVWEGYAA SKLIKAGFRS NSLDPNARH
//
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