ID A0A6I6IRU6_9RHOB Unreviewed; 942 AA.
AC A0A6I6IRU6;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:QGX99900.1};
GN ORFNames=EI983_17150 {ECO:0000313|EMBL:QGX99900.1};
OS Roseovarius faecimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=2494550 {ECO:0000313|EMBL:QGX99900.1, ECO:0000313|Proteomes:UP000428330};
RN [1] {ECO:0000313|Proteomes:UP000428330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MME-070 {ECO:0000313|Proteomes:UP000428330};
RA Nam Y.-D., Kang J., Chung W.-H., Park Y.S.;
RT "Complete genome sequence of Roseovarius sp. MME-070.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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; CP034348; QGX99900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6I6IRU6; -.
DR KEGG; rom:EI983_17150; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000428330; Chromosome.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02783; MopB_CT_2; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43598:SF5; DMSO REDUCTASE CHAIN A; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 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.
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:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000428330}.
FT DOMAIN 16..72
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 913..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 942 AA; 104740 MW; CD47691E87C77785 CRC64;
MTHQQPRINT SPKVSDEVRK TTCYMCACRC GINVHMKDGK VAYIEGNRDH PVNRGVLCAK
GSAGIMQVNA PSRLRAPLKR VGPRGSGQFE EISWDEALDI ATGWLEPLRE TAPEKLAFFT
GRDQSQSFTS FWAQNFGTPN YAAHGGFCSV NMAAAGIYTM GGAFWEFGQP DWDLTKLFMI
FGVAEDHDSN PIKMGIGKIK ARGARVIGVN PIRSGYNAVA DDWVGITPGT DGLFILALVH
ELLKAGKIDL DYLARYTNAP VLVNRDSKSP DYGLFLRDED GKPQVVDRVT GKLTAFDKPG
VKPDLHATYR HAGITHRPVM HLIASRYLDK QYAPEAVAER CGIKAEKIKA IAAEIARVAF
EEEVVLEREW TDFRGETHKV MRGRPVSFHA MRGISAHSNG FQTCRALHVL QILLGSVETP
GGFRFKPPYP KPVSAHPSPH CKVTPGKPLN GPHLGFVRGP ADLALKDDGT PARIDKAFTW
ENPMSAHGLM HMVISNAHAG DPYKIDTLFL YMANMSWNSS MNTSGVIDML TDTDENGDYV
IPRIIYSDAY SSEMVAYADL ILPDTTYLER HDCISLLDRP ICEADGAADA IRWPVIEPDR
DVRGFQTVLV QLANKMKLPG FTNEDGSAKY VDYADYITNH ERKPGIGPLA GWRLGKTGLT
HGRGEPNGSQ IQSYIANGGF FIKHVPDNAA YMKPWNMGYQ DWAVELGLFD SPQPYIFDLY
VETMRHFQLA AEGHGERQPP DHLRERIKKT MDPLPIWYPP FEDDHVDPDE YDVHALTQRP
MAMYHSWGTQ NAWLRQIHGH NPLYLPTKIW EKHGFATGDW ARVSSVHGEI TVPVAHMAAL
NDNTVWTWNA IGKRKGAWAL KDDAPEATKG FLLNHLIHEL LPPKGDGLRW SNSDPITGQA
AWFDLRVKIE KAPAPEESQP SLPPIASPVG TGPDELTWKV GK
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