ID A0A1I4IZE9_9BURK Unreviewed; 943 AA.
AC A0A1I4IZE9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=SAMN02982985_00836 {ECO:0000313|EMBL:SFL59343.1};
OS Rugamonas rubra.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Rugamonas.
OX NCBI_TaxID=758825 {ECO:0000313|EMBL:SFL59343.1, ECO:0000313|Proteomes:UP000199470};
RN [1] {ECO:0000313|EMBL:SFL59343.1, ECO:0000313|Proteomes:UP000199470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43154 {ECO:0000313|EMBL:SFL59343.1,
RC ECO:0000313|Proteomes:UP000199470};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
CC molybdopterin-containing oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00007023}.
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DR EMBL; FOTW01000005; SFL59343.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4IZE9; -.
DR STRING; 758825.SAMN02982985_00836; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000199470; 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; cd02790; MopB_CT_Formate-Dh_H; 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; IPR041925; CT_Formate-Dh_H.
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 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 PIRSF; PIRSF036643; FDH_alpha; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 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; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 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:UP000199470}.
FT DOMAIN 11..89
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 143..172
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 186..215
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 222..277
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 943 AA; 101286 MW; AC933E4B5E5592F6 CRC64;
MSPRASRPAG APLSFELNGR QVAADAGETL LEVADREGVA IPRLCHRDGM ADVGNCRACM
VEIAGERVLA PSCCRHPAEG MRVSTDSARA VAAQKLVLEL LLADMPATAH GRRNELDEWA
AALGVGRPRF APRVQPPRDL SHAAIAVNLD ACIQCTRCVR ACRDEQVNDV IGLAFRGDRA
AIVFDMADAM GESSCVACGE CVQACPTGAL APARGAALAE ADQQVASVCP YCGVGCQLTY
HVSDNRIAHV EGRDGPANHG RLCVKGRYGF DYANHPQRLT VPLVRRADAP PKRGDAEMDP
SRVMELFREA SWDEALALAG GGLARLRDSH GKGALAGFGS AKGSNEEAYL FQKLVRTGFG
SNNVDHCTRL CHASSVAALL EGIGSAAVSN PVRDVAKAEV VIVIGANPSV NHPVAATWIK
NAVRGGTRLI VCDPRRSELS RLAHRYLQFT PDTDVALLNA MMHVIVAEDL VDRDFIAART
VGYAELERNV AAYSPELMAP ICGVPAETIR YVARLYASSK ASMILWGMGI SQHVHGTDNA
RCLIALALMT GQIGRPGTGL HPLRGQNNVQ GASDAGLIPM MYPDYQRVDN PAARARFERA
WGVALDPRPG LTVVEVMHAI TRGEVRGMYI MGENPAMSDP DANHARASLA ALQHLVVQDI
FLTETAYLAD VILPASAFPE KTGSFTNTDR LVQMGRQALQ PPGQARQDLW IIVEMAKRLG
LDWRYSGPAE VFEEMRRTMP SIAGISWERL EREHAVTYPC LHEGDPGEAV VFTASFPRET
GRARFVPADI IPADERPDAD YPLVLITGRQ LEHWHTGSMT RRSAVLDALE PDPVALVHPL
DLAALGGRPG DVLTLESRRG RVALYARADD SSPRGAVFVP FCYYEAAINK LTNAALDPFG
KIPEFKYCAV RATLGGTLAA QGSFGGGQVL DALGEGPTAE PQP
//
