ID D6V3B4_9BRAD Unreviewed; 1247 AA.
AC D6V3B4;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Nitrate reductase, alpha subunit {ECO:0000313|EMBL:EFI52444.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:EFI52444.1};
GN ORFNames=AfiDRAFT_0430 {ECO:0000313|EMBL:EFI52444.1};
OS Afipia sp. 1NLS2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=666684 {ECO:0000313|EMBL:EFI52444.1, ECO:0000313|Proteomes:UP000004041};
RN [1] {ECO:0000313|EMBL:EFI52444.1, ECO:0000313|Proteomes:UP000004041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1NLS2 {ECO:0000313|EMBL:EFI52444.1,
RC ECO:0000313|Proteomes:UP000004041};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Prakah O.,
RA Elkins J.G., Brown S.D., Palumbo A.V., Hemme C., Zhou J., Watson D.B.,
RA Jardine P.M., Kostka J.E., Green S.J., Woyke T.J.;
RT "The draft genome of Afipia sp. 1NLS2.";
RL Submitted (MAY-2010) 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:EFI52444.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADVZ01000001; EFI52444.1; -; Genomic_DNA.
DR RefSeq; WP_009337376.1; NZ_ADVZ01000001.1.
DR AlphaFoldDB; D6V3B4; -.
DR eggNOG; COG5013; Bacteria.
DR Proteomes; UP000004041; 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: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.
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:EFI52444.1}.
FT DOMAIN 43..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1247 AA; 139691 MW; CFE61F587AA57A78 CRC64;
MSHFLDRLSF FTKTRTEFAG GHGITTTEDR SWEDGYRKRW QHDKIVRSTH GVNCTGSCSW
KVYVKGGIVT WETQQTDYPR TRPDLPNHEP RGCPRGASYS WYLYSGNRVK YPLVRSRLLK
LWRAARATLT PVAAWKSIVE NPEKRAAYTK RRGLGGFVRA NWDEVNEIIG AANAYTVKAH
GPDRVFGFSP IPAMSMVSYA SGARYLSLLG GVCMSFYDWY CDLPPASPQT WGEQTDVPES
ADWYNAGFLI LWGSNVPQTR TPDAHFYTEA RYKGAKSVVI CPDYSEASKF ADMWMSPKQG
TDAAVAMAMG HVILREFHID RKTAYFDDYM RRYSDMPMLV RLVKQGDHYI PDRFVRASDF
VDGLNEANNP EWKTVAYDEV SGGIVAPNGS IGFRWGEKGN WNLEEKAAGG DTRLRMSLMD
IQDDVAKVGF PYFGNREHDH FRGTDHPGVL TRNIPVKTLQ LADGETLVAS VFDLFVANYG
IDRGLGGENI AKGYDEIEPY TPAWAEQISG VPRDQIITVA REFARNAEKT HGRSMVIVGA
GLNHWYHMDM NYRGIINMLV MCGCVGQSGG GWSHYVGQEK LRPQSGWVPL AFGLDWSRPP
RQMNSTSAFY AHTDQWRYET LDVKDVLSPT APMGPWDGAL IDYNVRAERM GWLPSAPQLQ
TNPLDVAMQV EASGMEAKDY VAKALKSGEL KMSCEDPDNP KNWPRNLFVW RSNLLGASGK
GHEYFLKHLL GTSHGVIGKD LGDVGGRKPS EVAWHEEAPE GKLDLLVTLD FRMSTTCMYS
DIVLPTATWY EKNDLNTSDM HPFIHPLTAA IDPVWESRSD WEIYKGIAKS FSQVAPEVLG
VEKDVVLTPI MHDSPGEIAQ PFDVKDWKKG EIDPIPGKTM PAVAVVERDY PNLYKQFTSL
GPLMSKLGNG GKGMNWNTEH EVALLKRLNG VVTEEGPSKG LPKIDTDIDA CEVLLSLAPE
TNGEVAVKAW SSLGTFTGRD HTHLAIPKED EKIRFRDVVA QPRKIISSPI WSGLESESVC
YNACYTNVHE LIPWRTLTGR QQLYQDHLWM RAFGEGFCVY RPPIDTKSVK PVIDRKPNGN
KSIVLNFLTP HQKWGIHSTY TDNLLMLTLS RGGPIVWISE IDAKSAGLVD NDWIEVFNTN
GALVARAVVS QRVRQGMCMM YHAQEKIVNM PGSEQTGQRG GIHNSVTRVV LKPTHMIGGY
VQQAYGFNYY GTVGSNRDEF VIVRKMTKVD WLDEPVAASS ASLEAAE
//
