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Database: UniProt
Entry: A0A1H6Y0C4_9FIRM
LinkDB: A0A1H6Y0C4_9FIRM
Original site: A0A1H6Y0C4_9FIRM 
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
//
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