ID A0A176Z6X8_9BRAD Unreviewed; 921 AA.
AC A0A176Z6X8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=AYJ54_39785 {ECO:0000313|EMBL:OAF15512.1};
OS Bradyrhizobium centrolobii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1505087 {ECO:0000313|EMBL:OAF15512.1, ECO:0000313|Proteomes:UP000076959};
RN [1] {ECO:0000313|EMBL:OAF15512.1, ECO:0000313|Proteomes:UP000076959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR 10245 {ECO:0000313|EMBL:OAF15512.1,
RC ECO:0000313|Proteomes:UP000076959};
RA Simoes-Araujo J.L.Sr., Barauna A.C., Silva K., Zilli J.E.;
RT "Draft Genome Sequence of the Strain BR 10245 (Bradyrhizobium sp.) isolated
RT from nodules of Centrolobium paraense.";
RL Submitted (MAR-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}.
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:OAF15512.1}.
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DR EMBL; LUUB01000022; OAF15512.1; -; Genomic_DNA.
DR RefSeq; WP_063696443.1; NZ_LUUB01000022.1.
DR AlphaFoldDB; A0A176Z6X8; -.
DR STRING; 1505087.AYJ54_39785; -.
DR OrthoDB; 9816402at2; -.
DR Proteomes; UP000076959; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 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: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:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
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; 101630 MW; 9436600ABB92975C CRC64;
MTKITFELDG KQVEANSGET IWQVAKRQGR DIPHLCYSPE PDYRPDGNCR ACMVEIEGER
VLAASCKRTP SVGMKVKTES ARAVAAQKMV MELLVADQPA RETSHDPDSK FWHWAETTGV
TESRFPAAER WATDASHPAM RVNLDACIQC GLCVRACREV QVNDVIGMAY RNHDSKIVFD
FDDPMGESTC VACGECVQAC PTGALMPAVM LDDKQTRVTY ADKKVDSLCP FCGVGCQVTY
QVKDDKVIYA EGRDGPANHN RLCVKGRFGF DYIHHPHRLT KPLVRLPNAK KDANDQVDPA
NPFTHFREAS WEEALDIAAK GLVRIRDEKG VKALAGFGSA KGSNEEAYLF QKLVRTGFGS
NNVDHCTRLC HASSVAALFE GLSSGAVSAP FSAAMDAEVI WVIGANPAVN HPVAATFIKN
ATKQGAKLFV MDPRRQSLSR HATMHLQFKP GSDVALLNAM INTIITEGLT DDQYIAGYTE
GFEDLKEKIK EFTPEKMEPI CGIPAQTLRE VARTYARAKS SIIFWGMGIS QHVHGTDNAR
CLIALALITG QVGRPGTGLH PLRGQNNVQG ASDAGLIPMF LPDYQPVGRD DMRGSFEKLW
GQELDPVRGL TVVEIMNAIH AGEIKGMYIE GENPAMSDPD LQHAREALAM LDHLVVQDLF
VTETAFHADV ILPASAFAEK EGSFTNTDRR VQLARQVIRP PGDARQDLWI IQEIGKRMGL
PWNYSGPGEV YTEMAELMPS LKNISWERLV REGAVTYPAD DPNKPGNEII FTTGFPTASG
RGKIVPAKVI PPDELPDDEY PMVLSTGRVL EHWHTGSMTR RAQVLDQIEP EAVAFMSPKD
MRKKKLTPGD FIRLETRRGA VEVKVRSDRD VPENMVFMPF CYAEAAANLL TNPALDPFGK
IPEFKFCAAR AERAEMRDAA E
//