ID A0A1S8FHV5_9BURK Unreviewed; 945 AA.
AC A0A1S8FHV5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=B0B52_09855 {ECO:0000313|EMBL:OOG42949.1};
OS Polaromonas sp. A23.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1944133 {ECO:0000313|EMBL:OOG42949.1, ECO:0000313|Proteomes:UP000218978};
RN [1] {ECO:0000313|EMBL:OOG42949.1, ECO:0000313|Proteomes:UP000218978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A23 {ECO:0000313|EMBL:OOG42949.1,
RC ECO:0000313|Proteomes:UP000218978};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) 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}.
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:OOG42949.1}.
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DR EMBL; MUNO01000018; OOG42949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8FHV5; -.
DR STRING; 1944133.B0B52_09855; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000218978; 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:UP000218978}.
FT DOMAIN 15..93
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 147..176
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 190..219
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 226..281
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 945 AA; 103059 MW; C3317F930E79B90C CRC64;
MNAITRQELA ELDAPLVTFS LNGREVQGRA NESLLQVAKR EGVEIPHLCF KEGMEAVGNC
RSCMVEINGE RVLAPSCCRA PAAGMKVVTD SERAVASQKL VLELLLSDMP EKEYTRNNEV
DQWAAKIGVG KPRFEARQQV RQDLSHPAIA VNLDACIQCT RCLRACRDEQ VNDVIGLAFR
GDQAKIVFDM DDAMGVSTCV ACGECVQACP TGALMPAREA ALTVPDKQVE SVCPYCGVGC
QLTYNVKDDK ILFVEGRDGP ANHERLCVKG RYGFDYAHHP HRLTKPLIRR EGMPKTGDFT
MDPDRVMDVF REASWEEALE FAGGKLAAIR DQHGKKSLAG FGSAKGSNEE AYLFQKLVRT
GFGSNNVDHC TRLCHASSVV ALLEGIGSGA VSNPVMDVTK ADVVVIIGAN PTVNHPVAAT
WIKNAVKNGT KLIVMDPRRS DLTRVAHRHL QFKPDTDVPM LNAMMNVIVT EGLVDQAFID
SRTIGYEELR KNVEGYTPEL MAPICGIDAD TLRYVARLFA TSKGSMILWG MGVSQHVHGT
DNARCLIALS LMTGQIGRPG TGLHPLRGQN NVQGASDAGL IPMMFPDYQH VSSPAVRASF
EKAWKVAPGS LDDQVGLTVV EVMHAIKKGG IKGMYVQGEN PAMSDPDANH AREALAALDH
LVVQDIFLTE TAYLADVILP ASAFPEKDGS FTNTDRLVQM GRKAINPPGD ARQDLWIIMQ
IANRLGCGWD YKHVSEVFDE MRHTMPSIGG ITWERLDREH SVTYPCMKEG DPGQSVVFVE
DFPREGGRAK FVPADIIPAD ERPDTEYPMV LITGRQLEHW HTGSMTRRAT VLDAIEPDPV
ALVHPLDLAA MGGKPGDVVT IESRRGKVEL YARADESSPR GAVFVPFCYY EAAVNKLTNA
ALDPFAKIPE FKYCAIRVSL GGVPPVQDSY GGGQAMKNSI ALAGI
//
