ID A0A4Y7RM54_9FIRM Unreviewed; 683 AA.
AC A0A4Y7RM54;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Formate dehydrogenase subunit alpha {ECO:0000313|EMBL:TEB09901.1};
DE EC=1.17.1.9 {ECO:0000313|EMBL:TEB09901.1};
GN Name=fdhA_3 {ECO:0000313|EMBL:TEB09901.1};
GN ORFNames=Pmgp_02813 {ECO:0000313|EMBL:TEB09901.1};
OS Pelotomaculum propionicicum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=258475 {ECO:0000313|EMBL:TEB09901.1, ECO:0000313|Proteomes:UP000297597};
RN [1] {ECO:0000313|EMBL:TEB09901.1, ECO:0000313|Proteomes:UP000297597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGP {ECO:0000313|EMBL:TEB09901.1,
RC ECO:0000313|Proteomes:UP000297597};
RX PubMed=30126076; DOI=.1111/1462-2920.14388;
RA Hidalgo-Ahumada C.A.P., Nobu M.K., Narihiro T., Tamaki H., Liu W.T.,
RA Kamagata Y., Stams A.J.M., Imachi H., Sousa D.Z.;
RT "Novel energy conservation strategies and behaviour of Pelotomaculum
RT schinkii driving syntrophic propionate catabolism.";
RL Environ. Microbiol. 20:4503-4511(2018).
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}.
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:TEB09901.1}.
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DR EMBL; QFFZ01000036; TEB09901.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y7RM54; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000297597; 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:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
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; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 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 SMART; SM00926; Molybdop_Fe4S4; 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; 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:ARBA00022485};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:TEB09901.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000297597}.
FT DOMAIN 54..110
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 683 AA; 75882 MW; 25E45B282C826086 CRC64;
MKQRISRRNF LKYLGLGTAG TALLEGATAI PAFAGTAEDK LPTFEMGPLK IKKAKETASV
CAFCGVGCGL IVYSEGDRVI HIEGDPDNPN NEGTMCSKGI ALGDANTIVD KNRKRVVNDR
RIMDVLYRAP YSTKWEKKDW DWALAEIAKR VKKTRDESFE EKDAKGVTVN RTQAIAHIGS
ASCDNEENYL FQKMMRSLGV INFDHHARLC HSSTVTGLAQ SFGRGVMTNS FTDYKNTDVF
LIIGANPAEN HPQIMRHLGM AVTQRGAKVI VVDPRFTKTA AKADIYAQHR PGTDIAFLYG
MMNYAIQNGL YFYDYVLNYT NASYLVSPDY ALNEGVFTGL TEKDGKLSYD NKSWQYQKDG
DTIKKDPTLQ DPMCVFQILK KHVARYDIKT VSRITGTPED TFKKVCDLYC STGKPDKAGN
LIYAMGMTQH TYGAQNVRAT AMLQLLLGNI GIAGGGVNAQ RGESNVQGSS DQGILYANLT
GYVGAPSAAA HANLKEYLEK ETPKTSFWSN KPKFLISMLK AWYGDKATQE NDFCFDYLPK
HTGSDHSHMA IFEKMAEGSI KGYFAWGQNP AVGGPNVIAA RKAMENLDWM VAVDLFETET
AAFWHRPGAN PADIKTEVFL LPTAFSYEKE GTVANSSRWI QWRWKAVEPP GQAKSDLWIA
YEIFKAVRKE YQAGGKFPAP FCF
//
