ID C7RBW4_KANKD Unreviewed; 1250 AA.
AC C7RBW4;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=nitrate reductase (quinone) {ECO:0000256|ARBA:ARBA00012500};
DE EC=1.7.5.1 {ECO:0000256|ARBA:ARBA00012500};
GN OrderedLocusNames=Kkor_1343 {ECO:0000313|EMBL:ACV26756.1};
OS Kangiella koreensis (strain DSM 16069 / KCTC 12182 / SW-125).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Kangiellales; Kangiellaceae;
OC Kangiella.
OX NCBI_TaxID=523791 {ECO:0000313|EMBL:ACV26756.1, ECO:0000313|Proteomes:UP000001231};
RN [1] {ECO:0000313|EMBL:ACV26756.1, ECO:0000313|Proteomes:UP000001231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16069 / KCTC 12182 / SW-125
RC {ECO:0000313|Proteomes:UP000001231};
RX PubMed=21304661; DOI=10.4056/sigs.36635;
RA Han C., Sikorski J., Lapidus A., Nolan M., Glavina Del Rio T., Tice H.,
RA Cheng J.F., Lucas S., Chen F., Copeland A., Ivanova N., Mavromatis K.,
RA Ovchinnikova G., Pati A., Bruce D., Goodwin L., Pitluck S., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Saunders E., Brettin T., Goker M., Tindall B.J., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Kangiella koreensis type strain (SW-125).";
RL Stand. Genomic Sci. 1:226-233(2009).
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; CP001707; ACV26756.1; -; Genomic_DNA.
DR RefSeq; WP_012801270.1; NC_013166.1.
DR AlphaFoldDB; C7RBW4; -.
DR STRING; 523791.Kkor_1343; -.
DR KEGG; kko:Kkor_1343; -.
DR eggNOG; COG5013; Bacteria.
DR HOGENOM; CLU_000422_14_1_6; -.
DR InParanoid; C7RBW4; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000001231; 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: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.
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:UP000001231}.
FT DOMAIN 43..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1250 AA; 141506 MW; 9F53C6953E4C3768 CRC64;
MSQFLDRLQF FKKKQSEFSN GHGEVTNESR AWENSYRQRW QHDKIVRSTH GVNCTGSCSW
KIYVKNGLVT WETQQTDYPR TRPDLPNHEP RGCPRGASYS WYLYSANRLK YPKVRKPLLK
LWREARLTRS PVEAWQSIVE DPEKANSYKT KRGLGGFIRS SWDEVNEIIA ASNVYTAKQY
GPDRIVGFSP IPAMSMVSYA AGSRYLSLIG GVCMSFYDWY CDLPPASPMT WGEQTDVPES
ADWYNSNYII AWGSNVPQTR TPDAHFFTEV RYKGAKTVSI TPDYAEVSKL TDEWLNPKQG
TDAALGMAFG HVILKEFHLE NPSEYFTDYV RRYTDMPMLV VLEDYEKGGY TAGKFLRSSD
LVDSLGQDNN PEWKTIAYDE NTNELVSPLG SIGYRWGEKG KWNIQDKEGK EGKDVKLQLS
LIGDDVASVS FPHFASDKSN QHWVSCEHNE VLNRNVPCKT ITLADGRTVK VATVYDLMIA
NYGIDRGLGG ENVASSYDDD IPFTPAWQEK ITGVKRDKVI RIAREFADTA HKTKGKAMII
VGAAMNHWYH MDMNYRGLIN MLMMCGCVGQ SGGGWAHYVG QEKLRPQTGW LPLAFGLDWS
RPPRQMNSTS FFYNHSSQWR HEKVSIHEVL SPLADKSQYP EHMLDYNIKA ERMGWLPSAP
QLDRNPLQIT RDAEAAGMDP KDYVVQELKN GNLRFASEAP DDPKNFPRNL FVWRSNLLGS
SGKGHEYMLK YLLGTKNGLM NDDLGTRGGF KPDEADWVEK GPEGKLDLVV TLDFRMSSTC
LYSDIVLPTA CWYEKDDLNT SDMHPFIHPL STAVDPAWEA RSDWDIYKGI AKKFSEVAEG
ELGIEKDLVT VPILHDTAGE LAQSDVKDWK KGECELIPGK TAPNMMVVER DYPNTYKKFT
SLGPLLEKLG NGGKGIGWNT DEEVEFLRKL NHTVLDEGVS EGQPQIETAI DAAEVVLSLA
PETNGNVAVK AWSALGEFTG LDHTHLALPK HEEKIRFRDI QAQPRKIISS PTWSGLEDEH
VSYNAGYTNV HEFIPWRTIT GRQQFYQDHL WMQAFGEQMV SYRPPINTKT IEYVKDKKPN
GNKEIVLNWI TPHQKWGIHS TYSDNLLMLT LSRGGPIIWL SELDAKEAGI EDNDWVEVFN
ANGAIACRAV VSQRVKQGMV MMYHAQERIV NVPGSEMTGT RGGHHNSVTR VVLKPTHMIG
GYAQQSYGFN YYGTVGCNRD EFVVVRKMDK VDWLDGPDGD VHPQPLPDEV
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