ID V2IYP6_9BURK Unreviewed; 1273 AA.
AC V2IYP6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Nitrate reductase A subunit alpha {ECO:0000313|EMBL:ESJ18274.1};
GN Name=narZ {ECO:0000313|EMBL:ESJ18274.1};
GN ORFNames=B551_0211635 {ECO:0000313|EMBL:ESJ18274.1};
OS Cupriavidus sp. HPC(L).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1217418 {ECO:0000313|EMBL:ESJ18274.1, ECO:0000313|Proteomes:UP000053474};
RN [1] {ECO:0000313|EMBL:ESJ18274.1, ECO:0000313|Proteomes:UP000053474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPC(L) {ECO:0000313|Proteomes:UP000053474};
RA Purohit H.J., Agarwal L.;
RT "Cupriavidus a Desert isolate.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESJ18274.1}.
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DR EMBL; AMPR02000164; ESJ18274.1; -; Genomic_DNA.
DR RefSeq; WP_023264100.1; NZ_AMPR02000164.1.
DR AlphaFoldDB; V2IYP6; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000053474; Unassembled WGS sequence.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000053474}.
FT DOMAIN 43..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 1252..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1273 AA; 142265 MW; 9EAC3A3FA20D2297 CRC64;
MSHFLDRLRY FSTERIAFSN GHGAVTDEDR KWEDGYRQRW QHDKIVRSTH GVNCTGSCSW
KIYVKGGIVT WETQQTDYPR TRPDLPNHEP RGCSRGASYS WYLYSANRLK YPLVRSALVR
LWRERRQSMG PVEAWASIVD DPQARRSYQA RRGLGGFVRS SWDEVNEIVA AANVHTIARH
GPDRVVGFSP IPAMSMVSYA AGARYLSLLG GVCLSFYDWY CDLPPASPQT WGEQTDVPES
ADWYNSTFIV MWGSNVPQTR TPDAHFMTEV RYRGTKVVSI FPDYSEGAKF GDIWLHPKQG
TDAALALAMG HVVLKEFHLA PGRSAYFLDY CRRYTDMPCL VRLVPHGDGY VPERLVRAAD
FDDALGQANR PEWKTVMIDE TTDRVVVPPG SAGFRWGQQQ DGKPGDDAGK WNLRMESADG
TPLVPRLSLA EAHDEAVDVQ FPYFGNVPHP HFPNTGHGSV LSRRIGARRI ATRNGDMLVA
TVYDLFIANY GLDQGLGGRD VAASYDDDIP YTPAWQEAIT GVRRADVIAV ARQFAENAHK
TEGKSMVILG AGLNHWFHMD MSYRAIINLL IMCGCVGKSG GGWSHYVGQE KLRPQTGWTP
LSFGLDWYRP PRQMNGTSFF YAHTDQWRYD PMDPGALLSP LADKSQFHGA PIDYNVRAER
MGWLPSAPQL LQNPLALGRT LADPAAAGSV VADGLKSGAL RLACEDPDDP RAFPRNLFVW
RSNLLGSSGK GHEYFLRHLL GTTHGVQGEQ IGEGRHGEVP RPEEVAWHEN APEGKLDLLV
TLDFRMSTTC MYSDVVLPTA TWYEKDDMNT SDMHPFIHPL SAAVDPAWQS KSDWEIFKGI
AKRFSELAEG HLGIERDVVL SPIGKDTPAE LAQPFDVRDW KRGECEPQPG RTMPSVTVVE
RDYPATYRRF TSLGPLMDRL GNGGKGIGWN TEDEVRWLGE LNQRTSDSDD ADHAGHAGQR
PRIDSAIDAA EVILSLAPET NGAVAVKAWQ ALSALTGIDH THLARSRADE RIRFRDIQAQ
PRKIISSPTW SGIESEHVSY NACYTNVHEL IPWRTLTGRQ QLYQDHAWMR AFGESLCVYK
PPIDTGSYAG MVGTRSNGNP EIVLNFITPH QKWGIHSTYT DNLLMLTLSR GGPIVWIAED
DARQAGIVDN DWIECYNANG ALCARAVVSQ RVPRGMVMMY HAQEKIVNTP GSEITGGRGG
IHNSVTRVSL KPTHMIGGYA QLSYGFNYYG TVGANRDEFL IVRKMRRVDW LDDAPPDPVN
PATEHRIREG EAR
//
