ID A0A1M7TV10_9RHOB Unreviewed; 966 AA.
AC A0A1M7TV10;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Formate dehydrogenase major subunit {ECO:0000313|EMBL:SHN74557.1};
GN ORFNames=SAMN05216200_11072 {ECO:0000313|EMBL:SHN74557.1};
OS Oceanicella actignis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Oceanicella.
OX NCBI_TaxID=1189325 {ECO:0000313|EMBL:SHN74557.1, ECO:0000313|Proteomes:UP000184066};
RN [1] {ECO:0000313|EMBL:SHN74557.1, ECO:0000313|Proteomes:UP000184066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10808 {ECO:0000313|EMBL:SHN74557.1,
RC ECO:0000313|Proteomes:UP000184066};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) 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 -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; FRDL01000010; SHN74557.1; -; Genomic_DNA.
DR RefSeq; WP_072748143.1; NZ_FRDL01000010.1.
DR AlphaFoldDB; A0A1M7TV10; -.
DR STRING; 1189325.SAMN04488119_101492; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000184066; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-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: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; 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; 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:UP000184066};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 65..121
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 966 AA; 107416 MW; 074DC9092BB67FE1 CRC64;
MLRKKSDGVA QGPRAASVLS RIASKSIDRR SFLRGSGLAV GGLAALGATG AGVTRARAQS
AADNVEIIKS VCTHCSVGCT VVAEVQSGVW VGQEPGWDSP FNMGAHCAKG ASVREHAHGE
RRLKYPTKLV DGEWVRISWD EAINEIGDKM LEIREKSGPD SVYWLGSAKH SNEQAYLFRK
FAAYWGTNNV DHQARICHST TVAGVANTWG YGAMTNSYND IHNSKAIFVI GGNPAEAHPV
SLLHILRAKE RNNAPLIVCD PRFTRTAAHA DEYVRFRPGS DVALVWGILW HIFENGWEDK
EFIRTRVWGM DQIRAEVAKW NPAETERVTG VPGAQLERVA RTLVNNRPGT VIWCMGGTQH
TNGNNNTRAY CILQLALGNM GTAGGGTNIF RGHDNVQGAT DLGVLSHTLP GYYGLSAGAW
AHWARVWGED LDWLKSRFAT LKGKDGKDKP LMNETGIPVS RWIDGVLEAK ENIDQPDNVR
AMVLWGHAPN SQTRLPEMKK AMEKLDLMVV VDPYPTVSAV LHDRKDGVYL LPACTQFETY
GSVTASNRSI QWREKVVDPL FESRPDHTIM AMFARKFGFA DRLFRNIEVQ ETDRGPEPKV
EDITREFNRG MWTIGYTGQS PERLRSHMQN QHTFDRTTLQ AVGGPNDGEY YGLPWPCWGT
PEMGHPGTPI LYDMSKPVSK GGLTFRARFG VERDGQSLLA EGVYSAGSEI RDGYPEFTMA
MLKELGWDKD LTDQERAVIE GIAGDKTNWK TDLSGGIQRV AIKHECAPFG NAKARAVVWT
FPDPVPLHRE PLYTNRRDLV ADYPTYEDRK FYRLPTLYAS IQKKDFSKDY PIILTSGRLV
EYEGGGDETR SNPWLAELQQ DMFVEVNTRD ANDLGIRDGQ MVWVEGPEGG KVKVKAMVTE
RVGAGVAFMP FHFGGWFQGE DRRSKYPKGA DPYVLGESTN TAQTYGYDSV TQMQETKATL
CKIWAA
//
