ID A0A0D6SFS4_9PSED Unreviewed; 958 AA.
AC A0A0D6SFS4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN ORFNames=SZ55_3589 {ECO:0000313|EMBL:KIV67308.1};
OS Pseudomonas sp. FeS53a.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1604022 {ECO:0000313|EMBL:KIV67308.1, ECO:0000313|Proteomes:UP000032531};
RN [1] {ECO:0000313|EMBL:KIV67308.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FeS53a {ECO:0000313|EMBL:KIV67308.1};
RA de Souza R., Sant'Anna F.H., Ambrosini A., Tadra-Sfeir M., Faoro H.,
RA Alvarenga S.M., Pedrosa F.O., Souza E.M., Passaglia L.M.;
RT "Genome of Pseudomonas sp. FeS53a associated with rice cropped in iron-
RT stressed soils.";
RL Submitted (JAN-2015) 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:KIV67308.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYFT01000058; KIV67308.1; -; Genomic_DNA.
DR RefSeq; WP_044409199.1; NZ_JYFT01000058.1.
DR AlphaFoldDB; A0A0D6SFS4; -.
DR PATRIC; fig|1604022.3.peg.2441; -.
DR Proteomes; UP000032531; 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; 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; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
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 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; 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:UP000032531}.
FT DOMAIN 22..100
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 100..139
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 162..193
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 206..234
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 241..297
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 958 AA; 104735 MW; 3E69F184ADA8C47F CRC64;
MIQIFDPAKD TDLGTPARQS EVQVSLSIDG REISVPAGTS VMRAAALLGT TIPKLCATDS
LEAFGSCRMC LVEIDGMRGY PASCTTPVTE GMVVRTQTPK LASLRRNVME LYISDHPLDC
LTCSANGNCE LQTVAGQVGL REVRYGYDGA NHLSDAKDTS NPYFDYDPSK CIVCNRCVRA
CEEVQGTFAL TIDGRGFDSR VAAAGGENFL DSECVSCGAC VQACPTATLM EKSVVEMGQP
ERSVITTCAY CGVGCSFRAE MKGNELVRMV PDKNGQANHG HSCVKGRFAW GYATHPDRIT
KPMIRKRITD PWQEVSWEEA VNYAAGEFRR LQLQYGRDAI GGITSSRCTN EETYLVQKLV
RAGFGNNNVD TCARVCHSPT GYGLKQTLGE SAGTQSFDSV MQADVILVIG ANPTDAHPVF
GSQLKRRLRE GARLIVIDPR RIDLVDSPHA RAELHLALRP GTNVAMLNAL AHVIVTEGLV
KQDFVDARCE PADFARWSAF VSRPEHAPEA LGPVCGVAPD AIRAAARLYA TGGNAAIYYG
LGVTEHSQGS TAVMGIANLA MATGNVGREG VGVNPLRGQN NVQGSCDMGS FPHELPGYRH
VSNEAVRAQF EQAWGVTLQP DPGLRIPNMF EAALGGSFKG LYCQGEDIAQ SDPNTQHVTA
ALSAMECVVV QDIFLNETAK FAHVFLPGSS FLEKDGTFTN AERRISRVRK VMEPLGGKAD
WEATVALANA LGYRMDYRHP SEIMDEIARL TPTFSRVSYA ELERHGSLQW PCNDAAPDGT
PTMHIDAFVR GKGRFMLTGY VPTEEKVNNR YPLLLTTGRI LSQYNVGAQT RRTDNVAWHE
EDRLEIHPSD AESRGIAEGD WVGVGSRAGQ TVLRARVTER VAPGVVYTTF HFPESGANVI
TTDNSDWATN CPEYKVTAVE VTKVFQPSEW QKRYQAFSDE QRRLLKERRR TERVEARR
//
