ID A0A4Y9T1L9_9BURK Unreviewed; 933 AA.
AC A0A4Y9T1L9;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=E4O92_06810 {ECO:0000313|EMBL:TFW33446.1};
OS Massilia horti.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=2562153 {ECO:0000313|EMBL:TFW33446.1, ECO:0000313|Proteomes:UP000297258};
RN [1] {ECO:0000313|EMBL:TFW33446.1, ECO:0000313|Proteomes:UP000297258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ONC3 {ECO:0000313|EMBL:TFW33446.1,
RC ECO:0000313|Proteomes:UP000297258};
RA Peta V., Raths R., Bucking H.;
RT "Draft genome of Massilia hortus sp. nov., a novel bacterial species of the
RT Oxalobacteraceae family.";
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=[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:TFW33446.1}.
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DR EMBL; SPUM01000040; TFW33446.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y9T1L9; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000297258; 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:UP000297258}.
FT DOMAIN 6..84
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 139..168
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 182..211
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 218..273
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 933 AA; 101371 MW; D6BE7EBC55795CA7 CRC64;
MNAILKTVTF EINGRQVEAM PHETLIEVAG REGIEIPHLC HKDGLEAVGN CRSCMVEIDG
ERVLAPSCCR HPSQGMKVTT DSPRAVAAQK MVLELLMSDM RQSGYTRENE VDLWAQKLGV
GLPRFPATRA QPQCDATHAA ITVNLDACIQ CTRCVRACRD EQVNDVIGLA FRGQDARIVF
DQADPMGAST CVACGECVAA CPTGALAPAR GAALDIPDKK VDSVCPYCGV GCQLTYNVKD
NKILYVEGRD GPANHGRLCV KGRYGFDYAH HPHRLTKPLI RREGFPKTGD FTLDPSRVLD
VFREASWEEA LELAGGKLAQ IRDQHGKHAL AGFGSAKGSN EEAYLFQKLV RTGFGSNNVD
HCTRLCHASS VAALLEGIGS GAVSNPVMDV TRAEVVIVIG ANPTVNHPVA ATWMKNAVRA
GTKLIVCDPR RSDLARHAHR YLQFKPDTDV ALLNAMMHVI VTERLVDRAF IDSRTIGIEE
LEKNVEGYSP EAMAPVCGID AETIRYCARL YATSKASMIL WGMGVSQHVH GTDNARCLIA
LALMTGQIGR LGTGLHPLRG QNNVQGASDA GLIPMMLPDY QRVDNPAARA RFEQAWGTAL
DPKPGLTVVE IMDAITRGEI RGMYIMGENP AMSDPDANHA RAALAALDHL VVQDIFLTET
AYLADVILPA SAFPEKTGTF TNTDRLVQLG RQAIDPPGEA KQDLWIIQQI ARRLGLPWNY
GHVSEVFDEM RRTMPSIGGI TWERLELDDA VTYPCLHEGD PGEPVVFAHD FPREGGRARF
VPADIIPANE RPDAEYPMVL ITGRQLEHWH TGSMTRRTAV LDAIEPDPVA LVHPLDMARL
GVKPGEVITI ASRRGQVALY ARADDSSPVG AVFAPFCYYE AAINRLTNPA LDPFGKIPEF
KYCAVRVTPG GTVAPQGSFG GGQILGDMAQ SQA
//
