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Database: UniProt
Entry: A0A176Z6X8_9BRAD
LinkDB: A0A176Z6X8_9BRAD
Original site: A0A176Z6X8_9BRAD 
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
//
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