ID A0A1H6Y0C4_9FIRM Unreviewed; 996 AA.
AC A0A1H6Y0C4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Formate dehydrogenase major subunit {ECO:0000313|EMBL:SEJ30255.1};
GN ORFNames=SAMN05660742_105209 {ECO:0000313|EMBL:SEJ30255.1};
OS Propionispira arboris.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Propionispira.
OX NCBI_TaxID=84035 {ECO:0000313|EMBL:SEJ30255.1, ECO:0000313|Proteomes:UP000199662};
RN [1] {ECO:0000313|EMBL:SEJ30255.1, ECO:0000313|Proteomes:UP000199662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2179 {ECO:0000313|EMBL:SEJ30255.1,
RC ECO:0000313|Proteomes:UP000199662};
RA de Groot N.N.;
RL Submitted (OCT-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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; FNZK01000005; SEJ30255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6Y0C4; -.
DR STRING; 84035.SAMN05660742_105209; -.
DR Proteomes; UP000199662; 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:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0047111; F:formate dehydrogenase (cytochrome-c-553) activity; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; 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:0045333; P:cellular respiration; IEA:InterPro.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 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; 2.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006443; Formate-DH-alph_fdnG.
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 InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; TIGR01553; formate-DH-alph; 1.
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 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; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 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:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000199662};
KW Selenocysteine {ECO:0000256|ARBA:ARBA00022933};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..996
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039302493"
FT DOMAIN 42..98
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 996 AA; 111017 MW; 6E1711F93092BC83 CRC64;
MPILTRRSFL KLMATGTAAA LWQGNKAVPA MASPQSYRLK DTKVAPSLCI YCGVGCGLLA
YSKDGKIVNV EGDPDNPNNE GGLCPKGASL AELYSSPRRL KKILYRAPYS DTWEEKEWSW
AIPEIAKRIK ATRDKSFTKT HNGVTVNRTE KLAQLGGASH DTDENYLLMK FAKSLGIVNL
EHQARICHSS TVGSLAPSFG RGAMTNSIPD VANADVILIC GGNPAENHPG VSRFINRARD
KGAIVISVDP RYTKSSVLAD LYAPIRPGTD VVFFNAIANY IMKNKKYFEP AVVNYTNASY
ILKDDFAFKE GYFSGWDETK NQYDFKSWDY QIDASGAPLR DKTLQNPQCV FQHMIRFYSR
YTPEMVEKTT GMKQDIFLKI SEVIASTGVP DKAATLLYAM GLTQHTHGVQ NIRAFAIVQL
LLGNLGIPGG GINAMRGESN VQGSTDNGLL YDALTGYLPA PTEQKHATLE DYLKNVKKPN
SFMENAPNFA VSLLKAWWGD KAQPENNFCY EYLPKYSRPH SFMDIFDDMY AGGIEGMMLW
GMNPVVSGPN YNKQGAALEK LDWLMAADLF ESETHRFWKR PGVDPKTIKT EVFLLPAAGM
MEKDGSATNT SRWLQIRYKS VEPIADSKED SVMIHLLVEE LKRLYAEDAN AVFPDPIRDL
TWGYGGEHHD TERVFREMNG WTVGDKKQLS GFAQLKGDGS TASGNWIYCG MYPPEGNLAR
RRIPEKSGIG IHAQWAWAWP MNRRILYNRA GCDLAGKPFS DKKELIHWDS LQNKWTGMDV
PDFIANRAPS APLGDAPFLM IPYGLGRLFV PTGMVCDGPI PEHYESYESP VHNTFSKVQS
NPVAITFNSV FDKKSEVDDD NFPYVGTTYR LCEHYQSGNI TRKIKVTTEA APEAFVEIDP
DLAKEKGIKN GEFVELSSIR GTLKVKAFVT PRLQPYTIDG KKVHVVGMPW NYGFIGIDPL
ADGNLVQIAN MLTPAVGDPN TRIPEYKSFK VNVRRI
//