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Database: UniProt
Entry: A0A097R4W6_HAFAL
LinkDB: A0A097R4W6_HAFAL
Original site: A0A097R4W6_HAFAL 
ID   A0A097R4W6_HAFAL        Unreviewed;      1255 AA.
AC   A0A097R4W6;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE            EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN   Name=narZ {ECO:0000313|EMBL:AIU73775.1};
GN   ORFNames=AT03_16195 {ECO:0000313|EMBL:AIU73775.1};
OS   Hafnia alvei FB1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Hafnia.
OX   NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU73775.1, ECO:0000313|Proteomes:UP000029986};
RN   [1] {ECO:0000313|EMBL:AIU73775.1, ECO:0000313|Proteomes:UP000029986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB1 {ECO:0000313|EMBL:AIU73775.1,
RC   ECO:0000313|Proteomes:UP000029986};
RX   PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA   Tan J.Y., Yin W.F., Chan K.G.;
RT   "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT   pathogenesis: a draft genome perspective.";
RL   Gut Pathog. 6:29-29(2014).
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; CP009706; AIU73775.1; -; Genomic_DNA.
DR   RefSeq; WP_025799843.1; NZ_CP009706.1.
DR   AlphaFoldDB; A0A097R4W6; -.
DR   KEGG; hav:AT03_16195; -.
DR   PATRIC; fig|1453496.5.peg.3315; -.
DR   eggNOG; COG5013; Bacteria.
DR   HOGENOM; CLU_000422_14_1_6; -.
DR   OrthoDB; 9759518at2; -.
DR   Proteomes; UP000029986; Chromosome.
DR   GO; GO:0009325; C:nitrate reductase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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: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; IPR006655; Mopterin_OxRdtase_prok_CS.
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:SF8; RESPIRATORY NITRATE REDUCTASE 1 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.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029986}.
FT   DOMAIN          43..107
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   1255 AA;  141059 MW;  C5CECBA0D1143255 CRC64;
     MSKFLDRFRY FKQKGETFAD GHGQELNVNR DWEDGYRSRW QHDKIVRSTH GVNCTGSCSW
     KIYVKNGLVT WETQQTDYPR TRPDLPNHEP RGCPRGASYS WYLYSANRVK YPMMRKRLMK
     LWREAKALHS DPVDAWGSIV SDSEKSKEYK QARGRGGFVR SSWKEVNELI AASNVYTAKQ
     YGPDRIIGFS PIPAMSMVSY AAGARYLSLI GGVCLSFYDW YCDLPPASPM TWGEQTDVPE
     SADWYNSSYI IAWGSNVPQT RTPDAHFFTE VRYKGTKTVA VTPDYAEIAK LCDHWLNPKQ
     GTDSAMALAM GHVILNEFHV QRQTEYFADY VRTYTDMPML VLLEQRAEGH YAAGRMLRAS
     DLVDGLGQEN NPEWKTVAIN QNGELTAPQG SIGYRWGEKG KWNLEQRDGV SGEEVKLQLS
     LLDNYDEIAE VGFPYFGGIK TGESDPFNSV ELKDVLLHKL PVKRLQLADG STALVTSVYD
     LTLANYGIER GLNDENCAQS YDDVKAYSPA WAELVTGVSK ENIVRIAREF AENAEKTHGR
     SMIIVGAGVN HWYHMDMTYR GLINMLIFCG CVGQSGGGWA HYVGQEKLRP QTGWTPLAFG
     LDWQRPPRHM NSTSFFYNHS SQWRYETVGT EELLSPMADK SRFSTSLIDL NVRAERMGWL
     PSAPQLGTNP LHIAEQARAA GLSPVDYTVK SLKEGSIRFA AEQPDDEKNF PRNLFVWRSN
     LLGSSGKGHE YMLKYLLGTE HGIQGQDLGQ QGGVKPEDVE WKDNAGEGKL DLVVTLDFRM
     SSTCLYSDIV LPTATWYEKD DMNTSDMHPF IHPLSAAVDP AWESKSDWEI YKGIADAFSR
     MCDGHLGKET DIVTLPIQHD SAAELAQPFG VKDWKKGECD LIPGKTAPHI IAVERDYPNT
     YARFTSLGPL MDTLGNGGKG ISWNTQTEVD FLKQLNYTQP DGAAAGRPKI ETAIDAAEVI
     LSLAPETNGQ VAVKAWQALS NITGRDHTHL ALNKEDEKIR FRDIQAQPRK IISSPTWSGL
     EDEHVSYNAC YTNVHELIPW RTLSGRQQLY QDHEWMRAFG ESLLVYRPPI DTRAAAPVMG
     KSPNGNKEKA LNFLTPHQKW GIHSTYSDNL LMLTLGRGGP IVWLSEDDAK ELGIEDNDWI
     EAFNANGALT ARAVVSQRIP AGMTMMYHAQ ERIVNIPGSE ITSQRGGIHN SVTRISPKPT
     HMIGGYAQLA YGFNYYGTVG SNRDEFVVVR KMNRIDWLDE EGNDYSQGSQ QEKAK
//
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