ID X6L5X5_9RHOB Unreviewed; 995 AA.
AC X6L5X5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Contig2, whole genome shotgun sequence {ECO:0000313|EMBL:ETA53636.1};
GN ORFNames=P279_02200 {ECO:0000313|EMBL:ETA53636.1};
OS Rhodobacteraceae bacterium PD-2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1169855 {ECO:0000313|EMBL:ETA53636.1, ECO:0000313|Proteomes:UP000023196};
RN [1] {ECO:0000313|EMBL:ETA53636.1, ECO:0000313|Proteomes:UP000023196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PD-2 {ECO:0000313|EMBL:ETA53636.1,
RC ECO:0000313|Proteomes:UP000023196};
RX PubMed=25700405;
RA Zheng L., Cui Z., Xu L., Sun C., Powell R.J., Hill R.T.;
RT "Draft Genome Sequence of Rhodobacteraceae Strain PD-2, an Algicidal
RT Bacterium with a Quorum-Sensing System, Isolated from the Marine Microalga
RT Prorocentrum donghaiense.";
RL Genome Announc. Announc.3:e01549-14(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: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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:ETA53636.1}.
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DR EMBL; AWRV02000002; ETA53636.1; -; Genomic_DNA.
DR AlphaFoldDB; X6L5X5; -.
DR PATRIC; fig|1169855.3.peg.397; -.
DR HOGENOM; CLU_000422_1_1_5; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000023196; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 3.
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; PS51318; TAT; 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 Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000023196};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 67..123
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 744..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 995 AA; 109594 MW; 1527115E46BE5D8E CRC64;
MLRKKTNGVA RRPQRTSILS EAANASVDRR AFLRGSGLAI GGLAAIAATG GTVQQASAAT
AAATGAVELK KSVCTHCSVG CTVMAEVQDG VWTGQEPGWD SPFNLGAHCA KGASVREHAH
GERRLKYPMK KVGGEWVRIS WEEAINEIGD QMMSIREESG PDSVYWLGSA KHSNEQAYLF
RKFAAYWGTN NVDHQARICH STTVAGVANT WGYGAMTNSY NDIHNSKAIF IIGGNPAEAH
PVSLLHVLRA KEQNNAPLIV CDPRFTRTAA HADEYVRFRP GSDVALVWGI LYHIFENGWE
DKEFIRTRVW GMDQIREEVM KWTPEEVERV TGTPGSQLKR VAMTLANNRP GTVIWCMGGT
QHTNGNNNTR AYCILQLALG NMGTAGGGTN IFRGHDNVQG ATDLGVLADT LPGYYGLAKG
SWQHWARVWE EDFDYLAGRF STIKGADGKD KPMMNITGIP VSRWIDGVLE AKENLEQPDN
TRAMVFWGHA PNSQTRLVEM KGAMEKLDLL VVVDPYPTVS AILHDRTDGV YLLPAATQFE
TRGSVTASNR SLQWREQVVA PLFESLPDHT IMHKFATKFG FADRMFRNIE VVDGEPVVED
LTREFNKGMW TIGYTAQSPE RLKKHMANQH TFDRTTLRAL GGPCDGDFYG MPWPAWGTPE
MNHPGSANLY DVSLPVAQGG MGFRARFGVE HEGDNLLAEG VAPAGSEIPD GYPEFTMQML
IDLGWDSDLT DEERAVIERV AGYEAPEEAG EGEPEVGETS QQGDRPSDYA AAVGGVNWKT
DLSGGIQRVA IAHGCAPYGN AKARAVVWTF PDPIPLHREP LYTNRRDLVA DYPTYEDKSF
WRVPTMYASI QKNDFSQDYP IILTSGRLVE YEGGGDETRS NPWLAELQQD MFVEINPRDA
NNLGVRDGAD VWVEGPEGGK VKVMAMVTER VGEGVAFMPF HFGGHFQGED QRSKYPDGAD
PYVLGESTNT AQTYGYDSVT QMQETKATLC KIMPA
//
