ID A0A259UBI9_9FIRM Unreviewed; 668 AA.
AC A0A259UBI9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Formate dehydrogenase H {ECO:0000313|EMBL:OZC15501.1};
DE EC=1.1.99.33 {ECO:0000313|EMBL:OZC15501.1};
DE EC=1.2.1.2 {ECO:0000313|EMBL:OZC15501.1};
GN Name=fdhF_4 {ECO:0000313|EMBL:OZC15501.1};
GN ORFNames=SPACI_48050 {ECO:0000313|EMBL:OZC15501.1};
OS Sporomusa acidovorans DSM 3132.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Sporomusa.
OX NCBI_TaxID=1123286 {ECO:0000313|EMBL:OZC15501.1, ECO:0000313|Proteomes:UP000216052};
RN [1] {ECO:0000313|EMBL:OZC15501.1, ECO:0000313|Proteomes:UP000216052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3132 {ECO:0000313|EMBL:OZC15501.1,
RC ECO:0000313|Proteomes:UP000216052};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Sporomusa acidovorans DSM 3132.";
RL Submitted (FEB-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 -!- 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:OZC15501.1}.
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DR EMBL; LSLL01000098; OZC15501.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A259UBI9; -.
DR STRING; 112900.SAMN04488499_100933; -.
DR Proteomes; UP000216052; 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; cd02766; MopB_3; 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 Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 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; IPR006655; Mopterin_OxRdtase_prok_CS.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:OZC15501.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000216052}.
FT DOMAIN 1..58
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 668 AA; 73313 MW; DD9D3E42114DFA23 CRC64;
MEVMRSVCPY DCPDTCGLLV HVENGRAIKV EGDPDHPFTR GMLCPKMGHY EKTVHSKRRI
VTPLLRSGSK GSGNFVEVSW DEAIERIAGN WKQIVNQHGA EAILPYSYAG TMGLVQRNAG
HPFFYRLGAS RLERTICSPA KGHGWSAVMG KTMAPHPNEI HKSDLIILWG IHALATDIHI
MHDITIARKR GAKVWLIDTY ETPTAKVADQ VIVVRPGTDG ALALGIMHVI ARDKLEDRNF
ISQHVQGYTE LQAAVLPDYS PETVSQITGI AAGEIEQLAR QYAAAKAPFI RLGSGLSRYG
NGAMTVRTIT CLPGIVGAWG KPGGGLLAGT STEAAFAIKA ITHEEFLEQP TRIINMNKLG
QALNEVTDPP IKSLYVYISN PAAIAPDQNR VLQGLAREDL FTIVHERFMT DTAKYADIVL
PATSSLEHSD LYRSYGNYVV QRAYPVIAPV GQAKSNWEVF SLLAGAMEIK EPFFSQSADE
LIDAMLRNPS PWLAKLPLQP LQAGRPLELP LPDGYKTQFK TPSGKIEILN PHEDDKLPRY
IKPHGDDAEF WLINSPDPRL LNSSFNEREE LTTANKMLLQ MNPEDAAGKG LKDGQLVFAS
NERGEVVFTL KISAKIPAGI VVAEGVWWLE HVPGNRSVNA LTSQRLTDKG KGSTFYDVKV
NVKAAGNA
//
