ID A0A0C4Y8B8_9BURK Unreviewed; 1267 AA.
AC A0A0C4Y8B8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Respiratory nitrate reductase alpha chain {ECO:0000313|EMBL:AJG19188.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:AJG19188.1};
GN ORFNames=RR42_m1791 {ECO:0000313|EMBL:AJG19188.1};
OS Cupriavidus basilensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG19188.1, ECO:0000313|Proteomes:UP000031843};
RN [1] {ECO:0000313|EMBL:AJG19188.1, ECO:0000313|Proteomes:UP000031843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G11 {ECO:0000313|EMBL:AJG19188.1};
RX PubMed=25977418;
RA Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA Chakraborty R., Arkin A.P., Deutschbauer A.;
RT "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated from the
RT Oak Ridge Field Research Center Site.";
RL Genome Announc. 3:0-0(2015).
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; CP010536; AJG19188.1; -; Genomic_DNA.
DR RefSeq; WP_043345876.1; NZ_CP010536.1.
DR AlphaFoldDB; A0A0C4Y8B8; -.
DR STRING; 68895.RR42_m1791; -.
DR KEGG; cbw:RR42_m1791; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000031843; Chromosome main.
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:UniProtKB-EC.
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; 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; 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:AJG19188.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031843}.
FT DOMAIN 43..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1267 AA; 141673 MW; DFD602F3D3C1B2D4 CRC64;
MSHFLDRLTY FSQPRESFSD GHGQTTGEDR TWEDAYRNRW QHDKIVRSTH GTNCTGSCSW
KIYVKGGIVT WETQQTDYPR TRADLPNHEP RGCARGASYS WYLYSANRVK YPMVRGRLLK
HWRSARAVAK SPVDAWAAVV EDDAARREYQ QQRGLGGFVR SSWDEVNELI AAANVYTIKK
HGPDRVIGFS PIPAMSMVSY AAGSRYLSLI GGVCMSFYDW YCDLPPASPQ TWGEQTDVPE
SADWYNSTFL IAWGSNVPQT RTPDAHFFTE VRYKGAKVVA VTPDYAEVSK LADLWLHPKQ
GTDAALAMAM GHVILKEFYF ERRSAYFDDY ARRYTDLPLL VALKEHTLPD GSKTLVPDRY
VRASDFPDAL GQANHPEWKT VGFDEQGKVA LPHGSIGFRW GPDGRPDAGK WNLESKEARQ
GEAVKLKLSV VEDGAQPHDI VDVGFPYFGG IDTPHFTSSK TAGDVIVRRV PAARLALQEA
GGQRETLVAT VFDLLAANYG VARGLPGEQQ GGAATGGYDD EVPYTPAWQE RITGVARQQV
IAVARQFADN ADKTRGKSMV IIGAAMNHWY HCDMNYRGII NMLMLCGCIG QSGGGWAHYV
GQEKLRPQTG WTALAFALDW IRPPRQMNST SFFYAHTDQW RYEKLGVDEI LSPLADPARY
SGSMIDYNVR AERMGWLPSA PQLQTNPLQV QRDAQARGMD TRDYVAQSLK DGSLKLSCED
PDHPANWPRN MFVWRSNLLG SSGKGHEYFL KHLLGTSHGV QGKDLGPDHA KPEEVRWHEQ
APEGKLDLLV TLDFRMSTTC MYSDIVLPTA TWYEKNDLNT SDMHPFIHPL STAVDPAWQA
RSDWEIYKGF AKTFSKVCAG HLGVEKEVVL TPLMHDTPAE LAQPFGVRDW KKGECDLVPG
QTAPQINVVE RDYPNTYQRF TALGPLMTRI GNGGKGIGWD TQSEVHALGE LNGTVSEAGV
SQGLPRIDTD IDAAEVVMML APETNGHVAV KAWQALSRIT GREHAHLALH REDEKIRFRD
IQAQPRKIIS SPTWSGLESE KVSYNAGYTN VHELIPWRTL SGRQQFYQDH PWMRDFGEGF
VSYRPPINLK NVDEMLGKKP NGHPEIALNF ITPHQKWGIH STYTDNLIML TLNRGGPVIW
LSEDDAGRAG IVDNDWVELF NANGAIAARA VVSQRIKPGM VMMYHAQEKI INTPGSEITG
LRGGIHNSVT RVVLKPTHMI GGYAQYSYGF NYYGTIGTNR DEFVVVRKMN RVDWLDEPAN
ADAPGAA
//
