ID A0A074J1Z3_9RHOB Unreviewed; 961 AA.
AC A0A074J1Z3;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=TP2_14675 {ECO:0000313|EMBL:KEO50509.1};
OS Thioclava pacifica DSM 10166.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thioclava.
OX NCBI_TaxID=1353537 {ECO:0000313|EMBL:KEO50509.1, ECO:0000313|Proteomes:UP000027432};
RN [1] {ECO:0000313|EMBL:KEO50509.1, ECO:0000313|Proteomes:UP000027432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10166 {ECO:0000313|EMBL:KEO50509.1,
RC ECO:0000313|Proteomes:UP000027432};
RA Lai Q., Shao Z.;
RT "Thioclava pacifica DSM 10166 Genome Sequencing.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000455};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005404}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
CC molybdopterin-containing oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00007023}.
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:KEO50509.1}.
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DR EMBL; AUND01000042; KEO50509.1; -; Genomic_DNA.
DR RefSeq; WP_038080128.1; NZ_AUND01000042.1.
DR AlphaFoldDB; A0A074J1Z3; -.
DR STRING; 1353537.TP2_14675; -.
DR eggNOG; COG3383; Bacteria.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000027432; Unassembled WGS sequence.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
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:UniProt.
DR GO; GO:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd00508; MopB_CT_Fdh-Nap-like; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 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 InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041924; Formate_Dh-H_N.
DR InterPro; IPR006478; Formate_DH_asu.
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; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000027432}.
FT DOMAIN 26..104
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 104..143
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 176..207
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 219..247
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 254..310
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 961 AA; 104613 MW; A5E7F513662AD3BE CRC64;
MKDLIIPDGI HGPKLSDMGT PAKKGAPVTL VIDGMDVTVP EGTSVMRAAA EAGITVPKLC
ATDMLEAYGS CRLCVVEIEG MRGTPASCTT PVRDGMVVKT QTEQLQRLRR GVMELYISDH
PLDCLTCAAN GDCELQDMAG AVGLREVRYA PGQNHVETRA AEGPNPLYIP RDDSNPYFFY
DPSKCIVCMR CVRACEEVQG TFALTVDGRG FDARISTGTD DFLNSDCVSC GACVQACPTA
TLQEKTVEEI GTPERAIITT CAYCGVGCSF EAQMRGDQLV RMVPWKDGKA NRGHSCVKGR
FAWGYANHGD RILHPMIRES ITDAWREVSW EEALDFAAKG IKAAQAKHGK DSVGVITSSR
CTNEETFLVQ KLARAVMGTN NTDTCARVCH SPTGYGLKQT FGTSAGTQDF DSVEQVDCAV
VIGANPTDGH PVFGSRLRKR LRQGAGLIVI DPRRIDLLES VHMGEGIHLP LRPGTNVAVL
TALAHVIVTE KLYDEAFIRE RCDWEEWSDY AEFAADPAHS PEAVEALIGV PAETLRQAAR
TYAAAPNGAI YYGLGVTEHS QGSTTVIAIA NLAMMTGNIG RPGVGVNPLR GQNNVQGSCD
MGSFPHELPG YRHVSDDAAR AVFETEWHTT LDPEPGLRIP NMLDAAVAGD FKAIYIQGED
ILQSDPDTHH VAAGLAAMDC VIVHDLFLNE TARYAHVFLP GSTFLEKDGT FTNAERRINM
VRKVMAPKAG LADWEATQAL ANALGAGWSY THPSQIMAEI ARTTPSFAGV TYELIDRIGS
VQWPCNETHP QGSPVMHEDG FVRGKGRFIR TAYVATEERT GPRFPLLLTT GRILSQYNVG
AQTRRTENSV WHDQDLLEIH PHDAEQRGIN EGDWVRLASR SGETSLRATI TDRVSPGVVY
TTFHHPDTQA NVVTTDNSDW ATNCPEYKVT AVQVALSNGP SDWQELYEAQ TKLTRRVEAA
E
//
