ID X7F841_9RHOB Unreviewed; 1050 AA.
AC X7F841;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:ETX29052.1};
GN ORFNames=RISW2_03665 {ECO:0000313|EMBL:ETX29052.1};
OS Roseivivax isoporae LMG 25204.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=1449351 {ECO:0000313|EMBL:ETX29052.1, ECO:0000313|Proteomes:UP000023430};
RN [1] {ECO:0000313|EMBL:ETX29052.1, ECO:0000313|Proteomes:UP000023430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25204 {ECO:0000313|EMBL:ETX29052.1,
RC ECO:0000313|Proteomes:UP000023430};
RA Lai Q., Li G., Shao Z.;
RT "Roseivivax isoporae LMG 25204 Genome Sequencing.";
RL Submitted (JAN-2014) 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: 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:ETX29052.1}.
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DR EMBL; JAME01000013; ETX29052.1; -; Genomic_DNA.
DR RefSeq; WP_043770097.1; NZ_JAME01000013.1.
DR AlphaFoldDB; X7F841; -.
DR STRING; 1449351.RISW2_03665; -.
DR PATRIC; fig|1449351.3.peg.2100; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR Proteomes; UP000023430; 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; 2.
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:UP000023430};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 66..122
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 757..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1050 AA; 116405 MW; 922ADDA29196C807 CRC64;
MLKRRTAPRP ARPAFAAEER AGVDRRSFLK RSGLAIGGLG AVAGSGGMVV RAQEAPGTEA
PGRPEAEWRK TVCPFCSVGC SIWAEVRDGV WTGQEPAFES PINQGTHCAK GAATREIALG
ERRLKYPMKR QDGEWVRISW DQALEEIGAR LTQIREESGP DAVEWLGSAK FSNEAAYLFR
KFAALWGTNN VDHQARICHS TTVAGVANSF GYGAMTNSYN DIRNSKSIII IGGNPAEAHP
VSMLHVLNGK ENGAPLIVVD PRFTRTAAHA DEYVRIRPGA DVGFLWGLAK IIFDNGWEDR
AYLESRVFGI DRIREEAARW TAEEVERVSG VPPEQLHRVA KTIAENRPGT LIWCMGLTQS
SIGNNKTRAA SVLQLILGNI GKSGGGANIF RGHDNVQGAT DLGVSCDTLP AYYGLNEGAW
KHWGRVWDID YDWMRGRFAS KEMMEAPGIP VSRWPDGILE DGDALDQPVP LRAVFFWGHA
SNSQTRGPDR KEAWKAADLV VVVDPYPTQT AIEADLEDGM YLLPSGTTME MAGSVTNSNR
SIQWREKVID PVFEAKIDTE ILYLLAERLG FSDEMFRHIA VEGNVPSPED TLREINRGTW
TIGYTGPSPE RLKAHMQQQD RFDSITLLGK GGDVDGDYYC LPWPSWGRPE QRHPGTPLLY
DLSKPVAEGG LPFRARWGVE HEGETLLAED SWTAGSEIED GYPEITVNML EALGWAEELT
DREKLMIVAV ASDRFRWEMF DMPDEDVRAA MDALEEEVRR SGGGGDGAPA QIDGSWQNSS
PDGGERMAPG EARSAFPNYP ESALTAIEAY LQANIQNEAT DNMSLPERIA RVNWKTDLSG
GVQRVAIAHG LAPFGNGKAR AVVWTFPDEV PLHREPLYTN RRDLLPQYAT FEDRRVWRLP
SLYRSIQEND YSRDFPLQLT SGRLVEYEGG GDETRSNPWL AEFQQQMFAE INPNDAGAAG
IEDGGWVWVA TPEGRIRVKA MVTRRVGPGT VFMPFHFAGM WMGEPIHERY PEGAKPYVVG
EASNTVQTYG YDIVTQMQET KATLCRVERA
//
