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
//