ID A0A1A9S122_9NEIS Unreviewed; 1226 AA.
AC A0A1A9S122;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN ORFNames=A7P95_02085 {ECO:0000313|EMBL:OAM30813.1};
OS Eikenella longinqua.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Eikenella.
OX NCBI_TaxID=1795827 {ECO:0000313|EMBL:OAM30813.1, ECO:0000313|Proteomes:UP000077885};
RN [1] {ECO:0000313|Proteomes:UP000077885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML02-A-017 {ECO:0000313|Proteomes:UP000077885};
RA Bernier A.-M., Bernard K.;
RT "Draft genome of Corynebacterium afermentans subsp. afermentans LCDC
RT 88199T.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001854};
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 -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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:OAM30813.1}.
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DR EMBL; LXSL01000012; OAM30813.1; -; Genomic_DNA.
DR RefSeq; WP_067590432.1; NZ_LXSL01000012.1.
DR AlphaFoldDB; A0A1A9S122; -.
DR STRING; 1795827.A7P95_02085; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000077885; Unassembled WGS sequence.
DR GO; GO:0009325; C:nitrate reductase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0008940; F:nitrate reductase activity; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR GO; GO:0042126; P:nitrate metabolic process; IEA:InterPro.
DR CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 1.
DR CDD; cd02750; MopB_Nitrate-R-NarG-like; 1.
DR Gene3D; 3.40.50.12440; -; 1.
DR Gene3D; 4.10.1200.10; nitrate reductase tail; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037943; MopB_CT_Nitrate-R-NarG-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; IPR006468; NarG.
DR InterPro; IPR028189; Nitr_red_alph_N.
DR InterPro; IPR044906; Nitr_red_alph_N_sf.
DR NCBIfam; TIGR01580; narG; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR PANTHER; PTHR43105:SF2; RESPIRATORY NITRATE REDUCTASE 2 ALPHA CHAIN; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF14710; Nitr_red_alph_N; 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.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 43..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1226 AA; 138894 MW; F371CA2DFA8A3BB0 CRC64;
MSHFLDRLTF FKQKREPFAN GHGILTTEDR KWEDAYRSRW SHDKVARSTH GVNCTGSCSW
KIYVKNGIIT WETQQTDYPR TRPDLPNHEP RGCPRGASFS WYVYSAQRIK YPMMRGALAE
LWREARQTKD PIEAWKWIVE DPERAKSYKS QRGLGGFVRS NWDEAYEMVA AANCYTIKKY
GPDRIIGFSP IPAMSMVSYA AGARYLGLIG GVPLSFYDWY CDLPPASPQT WGEQTDVAES
ADWYNSNYLL VWGSNIPMTR TPDAHFYTEV RYKGTKTVAV SSDFGEMTKF SDIWLAPRQG
TDAALSMAMG HVILKEFHID NPSDYFQDYC RRLTDMPVLV CLKEDGEGYR PEYTLRASQL
GGNFGEEKNP DWKVLAWNEK TDSLMLPNGS IGFRWDGSGK WNLETKAQDE QDVQAALSLK
TCADDVVRVG FDYFGGEFDE EKTFRKVPVK RITLADGSSQ LVATVFDLLV AQYGVDNGLG
DENVAKDYFD DKPYTPKWQE KHTGVKAEQV IQVAREFAQN AHDTKGRSMI IVGAGINHWY
YLDMNYRGII NMLMMCGTIG KSGGGWCHYV GQEKLRPQSG WAPLTFALDW HRPARQMAGT
AFFYGHTGQY RHETVSADEL LTTDAGDDMR RLTMIDYHAK AARMGWTPSA PQLETNPLDV
TDAAEKAGMN PVDYVVKGLK EGTLDMSCDD PENPKNWPRN MFVWRSNILG SSGKGHEFFL
KYLLGTQNGL LSNEEDCLKP TEVKQRDGVE GKLDLFALLD FRMNTTCLYG DVIFPTATWY
EKDDLNTSDM HPFIHPLTEA VQPLWQSKSD WEIYKGLAKK FSELAKDYLG VRKDIVLTPL
MHDSPQELGQ PFDPKDWKLG ECEPIPGKTM PAMTVVERDY GAVYEKFTAV GPLLEKVNNN
GKGMAWDTKH EVEFLRKLNG VQPEGAGKGQ PKLETAIDAA EMILTLAPET NGHVSKKAWQ
ALSKNTGRDH THLINSSEHT QIRFRDIVAQ PRKIVTSPIW SGVESEEVCY TAGYTNVHEL
IPWRTLTGRQ QFYQDHKWMR DFGAGFCVYR PAVDTKTTKQ LLGKMPNGNP EITLNFLTPH
QKWGIHSTYS ENLRMLTLSR GGPHVWISEI DAKKAGLVDN DWVEVFNTNG SIACRVIVSQ
RIPETMIVMP HAQEKLVHTP AAETTKKRGG IHNSVTKAVL NPTHLIGGYA QLAYGFNYYG
TVGSNRDEWV IVRKMKDIDW MDEPAE
//
