ID K8PMR5_9BRAD Unreviewed; 921 AA.
AC K8PMR5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=HMPREF9695_01186 {ECO:0000313|EMBL:EKS42094.1};
OS Afipia broomeae ATCC 49717.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=883078 {ECO:0000313|EMBL:EKS42094.1, ECO:0000313|Proteomes:UP000001096};
RN [1] {ECO:0000313|EMBL:EKS42094.1, ECO:0000313|Proteomes:UP000001096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49717 {ECO:0000313|EMBL:EKS42094.1,
RC ECO:0000313|Proteomes:UP000001096};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Afipia broomeae ATCC 49717.";
RL Submitted (APR-2012) 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:EKS42094.1}.
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DR EMBL; AGWX01000001; EKS42094.1; -; Genomic_DNA.
DR RefSeq; WP_006019907.1; NZ_KB375282.1.
DR AlphaFoldDB; K8PMR5; -.
DR PATRIC; fig|883078.3.peg.1223; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_0_5; -.
DR Proteomes; UP000001096; 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:UP000001096}.
FT DOMAIN 2..82
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 138..168
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 181..210
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 921 AA; 101606 MW; B27D88B0C2F5FF37 CRC64;
MTKIQFELDG KMVEAQPGES IWQVAKREGT EIPHLCYSPE PDYRADGNCR ACMVEIEGER
VLAASCKRMP NVGMKVKSAS ARAVSARKMV MELLVADQPA RETSHDPDSK FWSWADKVNV
TESRFPANDR WSSDTSHPAM SVNLDACIQC GLCVRACREV QVNDVIGMAY RNHDAKIVFD
FDDPMGESTC VACGECVQAC PTGALMPSAY LDANQTRTVY PDKQVDSLCP FCGVGCQVTY
EVKDEKIVYA EGRDGPANHN RLCVKGRFGF DYIHHPHRIT KPLVRLPNAK KSSTDQVDPA
NPFTHFREAS WEEALDIAAQ GLVKIRDEKG VKALAGFGSA KGSNEEAYLF QKLVRTGFGS
NNVDHCTRLC HASSVAALME GLNSGAVSAP FAAAADAEVI IVIGANPTVN HPVAATFIKN
AAKKGAKLIV MDPRRQTLSR HATMHLQFKP GSDVAMLNAM LHTIITEGLT DDQYIAGYTE
GFDDLKEKIK EFPPEKMEPI CGVPAETLRE VARMYATAKS SIIFWGMGIS QHVHGTDNAR
CLIALALITG QVGRPGTGLH PLRGQNNVQG ASDAGLIPMF LPDYQPVGRT DLRDPFEHLW
RHEIDPVRGL TVVEIMDAIH AGDITGMYIE GENPAMSDPD LQHARQALAM LDHLVVQDLF
VTETAFHADV ILPASAFAEK VGSFTNTDRR VQIARQVVKP PGDARQDLWI IQEIAKRMGL
DWNYSGPADV FHEMTQLMPS LKNITWERLE REGAVTYPVD DPFKPGNEII FTTGFPTESG
RGKIVPARVT APDEIPDEEY PMVLSTGRVL EHWHTGSMTR RSGVLDSIEP EAVAFMSPKD
MRRLNVWPGD FIKLETRRGA IEVKVRSDRD VPENMVFMPF CYAEAAANLL TNPALDPFGK
IPEFKFCAAR AERAEVRTAA E
//
