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Database: UniProt
Entry: A0A4R6DQM2_9RHOO
LinkDB: A0A4R6DQM2_9RHOO
Original site: A0A4R6DQM2_9RHOO 
ID   A0A4R6DQM2_9RHOO        Unreviewed;       988 AA.
AC   A0A4R6DQM2;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE            EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN   ORFNames=C7389_12414 {ECO:0000313|EMBL:TDN46854.1};
OS   Azoarcus indigens.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Azoarcus.
OX   NCBI_TaxID=29545 {ECO:0000313|EMBL:TDN46854.1, ECO:0000313|Proteomes:UP000295129};
RN   [1] {ECO:0000313|EMBL:TDN46854.1, ECO:0000313|Proteomes:UP000295129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12121 {ECO:0000313|EMBL:TDN46854.1,
RC   ECO:0000313|Proteomes:UP000295129};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAR-2019) 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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00005404}.
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:TDN46854.1}.
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DR   EMBL; SNVV01000024; TDN46854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R6DQM2; -.
DR   OrthoDB; 9810782at2; -.
DR   Proteomes; UP000295129; Unassembled WGS sequence.
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:0015942; P:formate metabolic process; IEA:InterPro.
DR   CDD; cd00207; fer2; 1.
DR   CDD; cd00508; MopB_CT_Fdh-Nap-like; 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; 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   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
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   Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR   PIRSF; PIRSF036643; FDH_alpha; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 1.
DR   SMART; SM00929; NADH-G_4Fe-4S_3; 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; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   PROSITE; PS51839; 4FE4S_HC3; 1.
DR   PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 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:UP000295129};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          36..114
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          114..153
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51839"
FT   DOMAIN          181..212
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          224..253
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          260..316
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   988 AA;  106844 MW;  31EEC05953E8E1E4 CRC64;
     MNHPDPQARL QPAATVAPIT FHRSPDLGTP ARESDTLVTL SIDGNEVTVP AGTSLMRAAG
     LAGCSVPKLC ATDSLEPFGS CRLCLVEIDG RRGYPASCTT PAEAGMVVRT QSPRLAELRR
     GVMELYISDH PLDCLTCAAN GDCELQDMAG VVGLREVRYG MTGNDNHFDA EHAAAPDTSN
     PYFTYDPAKC IVCNRCVRAC EETQGTFALT ISGRGFESRV TAGAGESFLG SECVSCGACV
     QACPTATLTE KTVIEQGQAE KSVVTTCAYC GVGCAFEAEV KGNEVVRMVP YKDGQANRGH
     SCVKGRFAWG YATHPDRIKS PMIRASIDEP WREVSWEEAI SHAASEFRRI QAEHGRGAVG
     GLTSSRCTNE ETYLVQKLIR AGFGNNNVDT CARVCHSPTG YGLGQTYGTS AGTQTFDSVQ
     YADVVMVIGA NPTDGHPVFG SRLKRRLRQG AKLIVIDPRA IDLVRSPHIA AAHHLKLRPG
     TNVAVINALA HVIVTEGLVD EAFVAERCDA ESFAMWRAFV ADPANSPEAL EATTGVPVAE
     LRGAARLYAT GRSDGTAADL ANRRPNGAIY YGLGVTEHSQ GSTMVMGIAN LAMATGNIGR
     EGVGVNPLRG QNNVQGSCDM GSFPHELPGY RHVSDPLTRA LFGEAWGVDI DPEPGLRITN
     MLEAALDGSF KGLYCQGEDI VQSDPNTQHV EAALREMECV VVQDIFLNET AKFAHVLLPG
     ASFLEKDGTF TNAERRISRV RKVMPPLAGK ADWEVTVDLA RALGYPMDYA HPSEIMDEIA
     RLTPTFAGVS YERLEELGSI QWPCNAAQPE GTPTMHVAGF VRGKGRFMPT RYVATEEKVN
     ARYPLILTTG RILSQYNVGA QTRRTPNNLW HAEDRLEIHP QDAEERGIHD GDWVGISSRA
     GETVLRATLT GRVQPGVVYT TFHFPESGAN VITTDNSDWA TNCPEYKVTA VQVVPVSKPS
     EWQARFQRFT RRQEDHLRAA SADGKVEV
//
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