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Database: UniProt
Entry: A8AG28_CITK8
LinkDB: A8AG28_CITK8
Original site: A8AG28_CITK8 
ID   A8AG28_CITK8            Unreviewed;      1247 AA.
AC   A8AG28;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE            EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN   OrderedLocusNames=CKO_01301 {ECO:0000313|EMBL:ABV12441.1};
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338 {ECO:0000313|EMBL:ABV12441.1, ECO:0000313|Proteomes:UP000008148};
RN   [1] {ECO:0000313|EMBL:ABV12441.1, ECO:0000313|Proteomes:UP000008148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696
RC   {ECO:0000313|Proteomes:UP000008148};
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) 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   -!- 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; CP000822; ABV12441.1; -; Genomic_DNA.
DR   RefSeq; WP_012132184.1; NC_009792.1.
DR   AlphaFoldDB; A8AG28; -.
DR   STRING; 290338.CKO_01301; -.
DR   GeneID; 45135412; -.
DR   KEGG; cko:CKO_01301; -.
DR   HOGENOM; CLU_000422_14_1_6; -.
DR   OrthoDB; 9759518at2; -.
DR   Proteomes; UP000008148; 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: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; 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.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 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:UP000008148}.
FT   DOMAIN          43..107
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   1247 AA;  140655 MW;  E81C138710D4279C CRC64;
     MSKFLDRFRY FKQKGETFAD GHGQLLETNR DWEDGYRQRW QHDKVVRSTH GVNCTGSCSW
     KIYVKNGLVT WETQQTDYPR TRPDMPNHEP RGCPRGASYS WYLYSANRLK YPLMRKRLMK
     MWRDAKKLHS DPVEAWASII EDADKAKSFK QARGRGGFVR SSWQEVNELI AASNVYTIKN
     YGPDRVAGFS PIPAMSMVSY ASGARYLSLI GGTCLSFYDW YCDLPPASPQ TWGEQTDVPE
     SADWYNSSYI IAWGSNVPQT RTPDAHFFTE VRYKGTKTVA VTPDYAEIAK LCDLWLAPKQ
     GTDAAMALAM GHVMLREFHL DNPSQYFTDY VRRYTDMPML VMLEERDGYY AAGRMLRAAD
     LIDALGQENN PEWKTVAINT RGDMVAPNGS IGFRWGEKGK WNLEQRDGTS GEETELQLSL
     LGSQDDIAEV GFPYFGGEGT EHFNKVELQN VLLHKLPVKR LQLADGTTAL VTTVYDLTMA
     NYGLERGLND ENCATSYDDI KAYTPAWAEQ ITGVPRAQIT RIAREFADNA DKTHGRSMII
     VGAGLNHWYH LDMNYRGLIN MLVFCGCIGQ SGGGWAHYVG QEKLRPQTGW QPLAFALDWQ
     RPARHMNSTS YFYNHSSQWR YETVTAQELL SPMADKSRYS GHLIDFNVRA ERMGWLPSAP
     QLGTNPLYIA REAEKAGMTA VDYTVKSLKE GSIRFAAEQP ENGKNHPRNL FIWRSNLLGS
     SGKGHEYMLK YLLGTENGIQ GKDLGMQGGV KPEEVEWQDN GLDGKLDLVV TLDFRLSSTC
     LYSDIVLPTA TWYEKDDMNT SDMHPFIHPL SAAVDPAWES KSDWEIYKGI AKKFSEVCVG
     HLGKETDVVT LPIQHDSAAE LAQPLDVKDW KKGECDLIPG KTAPHIIPVE RDYPATYERF
     TSIGPLMEKI GNGGKGIAWN TQSEMDLLRK LNYTKAEGPA KGQPMLNTAI DAAEMILTLA
     PETNGHVAVK AWAALSEFTG RDHTHLATNK EEEKIRFRDI QAQPRKIISS PTWSGLEDEH
     VSYNAGYTNV HELIPWRTLS GRQSLYQDHQ WMRDFGESLL VYRPPIDTRS VKAVMGEKSN
     GNPEKALNFL TPHQKWGIHS TYSDNLLMLT LSRGGPIVWM SETDAKDLGI EDNDWIEVFN
     SNGALTARAV VSQRVPAGMT MMYHAQERIV NLPGSEITQQ RGGIHNSVTR ITPKPTHMIG
     GYAQLAYGFN YYGTVGSNRD EFVVVRKMKN INWLDGEGND QVQESVK
//
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