ID A0A4R2NZ59_RHOAD Unreviewed; 1242 AA.
AC A0A4R2NZ59;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Respiratory nitrate reductase alpha subunit apoprotein {ECO:0000313|EMBL:TCP27593.1};
GN ORFNames=EV656_101502 {ECO:0000313|EMBL:TCP27593.1};
OS Rhodovulum adriaticum (Rhodopseudomonas adriatica).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=35804 {ECO:0000313|EMBL:TCP27593.1, ECO:0000313|Proteomes:UP000295733};
RN [1] {ECO:0000313|EMBL:TCP27593.1, ECO:0000313|Proteomes:UP000295733}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2781 {ECO:0000313|EMBL:TCP27593.1,
RC ECO:0000313|Proteomes:UP000295733};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) 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:TCP27593.1}.
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DR EMBL; SLXL01000001; TCP27593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R2NZ59; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000295733; 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.
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:UP000295733}.
FT DOMAIN 44..108
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1242 AA; 139733 MW; 67AB5D205A86EC9F CRC64;
MSHLLDRLNF LKPKELEKFS DGWGQVTKED RNWEDTYRNR WRHDKIVRST HGVNCTGSCS
WKIYVKSGIV TWETQQTDYP RTRADLPNHE PRGCQRGASY SWYLYSANRV KHPLVRGRLM
RMWRELRQTK SPIQAWAAIQ KDPALRAEYT RIRGKGGFVR ASWDEATEIV AAANAWTAKT
WGPDRVFGFS PIPAMSMVSY AAGSRYLSLL GGTCLSFYDW YCDLPPSSPQ TWGEQTDVPE
SADWYNAGFL LIWGSNVPQT RTPDAHFYTE ARYRGTKSAV ICPDYSEASK FGDIWLNPKQ
GTDSALAMAM GHVILREFHL DRQAPYFEDY ARKYTDMPML VRLEEKDGRF VPGRMLRADD
FDGHLGQTNN PDWKTVGFDD RTGDIVVPNG SAGFRWGEEG KWNLEERAGD REVSLRLSQI
LEEHHDEVVG VDFPYFGGAA HQHFVKCGHP DVLTRNIPAR RVKLADGEAL VVTVFDLFCA
NYGLDRGLGG EWIARSYDED LPYTPAWAEK ITGVPADKII TVAREFAMNA EKTQGKSMVI
LGAGLNHWYH MDMNYRGIIN LLVMCGCVGQ SGGGWSHYVG QEKLRPQTGW LPLAFALDWN
RPPRQMNGTS AFYAHTDQWR YETLNVREIL SPTAPEGDWD AALIDYNIRA ERMGWLPSAP
QLKTNPLEVA KAAKAAGQDP KDYVAEGLKS GALQMSCEDP DAPENWIRNL FVWRSNLLGS
SGKGHEYFIK HLLGTDNGVM GKDLGAEGRE KPKEAVWHDT APEGKLDLLV CIDFRMSTTA
VYSDVVLPTA SWYEKNDLNT SDMHPFIHPL QAAVDPAYES KSDWEIFKAI ARKFSEVAPE
ILGVETDIVQ APILHDTPGE LAQPHVRDWK KGECDLIPGK TAPNYVAVER DYPALYDRFV
SVGPLLDTLG NGGKGIGWNT EAEIHELAKL NGAWADGPAK GRPKIVTDID ATEVILMLAP
ETNGEVAVKA WQALEKPTGR HHAHLAEGQE HNKIRFRDIA AQPRKIISSP TWSGIESEEV
CYNAGYTNVH ELIPWRTVTG RQQLYQDHLW MRAFGEALCQ YRPPVDLKTI TAEVNPETDR
PHVVLNFITP HQKWGIHSTY TDNLHMLTLN RGGPVVWISE VDAKKAGIED NDWIEAFNVN
GALTARAVVS QRVKEGMTLM YHAQEKIVNT PGSEKTGIRG GIHNSVTRAV PKPTHMIGGY
AQLAYGFNYY GTVGSNRDEF VIVRKMNKVD WLDRPATQEA AE
//