ID Q88KV4_PSEPK Unreviewed; 960 AA.
AC Q88KV4;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN OrderedLocusNames=PP_2185 {ECO:0000313|EMBL:AAN67798.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488 {ECO:0000313|EMBL:AAN67798.1, ECO:0000313|Proteomes:UP000000556};
RN [1] {ECO:0000313|EMBL:AAN67798.1, ECO:0000313|Proteomes:UP000000556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440
RC {ECO:0000313|Proteomes:UP000000556};
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L., Beanan M., DeBoy R.T., Daugherty S., Kolonay J., Madupu R.,
RA Nelson W., White O., Peterson J., Khouri H., Hance I., Chris Lee P.,
RA Holtzapple E., Scanlan D., Tran K., Moazzez A., Utterback T., Rizzo M.,
RA Lee K., Kosack D., Moestl D., Wedler H., Lauber J., Stjepandic D.,
RA Hoheisel J., Straetz M., Heim S., Kiewitz C., Eisen J.A., Timmis K.N.,
RA Dusterhoft A., Tummler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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}.
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DR EMBL; AE015451; AAN67798.1; -; Genomic_DNA.
DR RefSeq; NP_744334.1; NC_002947.4.
DR RefSeq; WP_010953170.1; NC_002947.4.
DR AlphaFoldDB; Q88KV4; -.
DR STRING; 160488.PP_2185; -.
DR PaxDb; 160488-PP_2185; -.
DR GeneID; 83681292; -.
DR KEGG; ppu:PP_2185; -.
DR PATRIC; fig|160488.4.peg.2304; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_1_6; -.
DR OrthoDB; 9810782at2; -.
DR PhylomeDB; Q88KV4; -.
DR BioCyc; PPUT160488:G1G01-2326-MONOMER; -.
DR Proteomes; UP000000556; Chromosome.
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:UP000000556}.
FT DOMAIN 24..102
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 102..141
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 164..195
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 207..236
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 243..299
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 960 AA; 104886 MW; 364C24241EFEDA25 CRC64;
MINFFDPASD KSSDLGTPAR ESDVQVSLSI DGRAISVPAG TSVMRAAAML GTSIPKLCAT
DSLEAFGSCR MCMVEIEGMR GYPASCTTPV SEGMVVRTET PRLAGLRRNV MELYISDHPL
DCLTCSANGN CELQTVAGQV GLREVRYGYD GANHLDEKKD VSNPYFDYEP SKCIVCSRCV
RACEDIQGTF ALTITGRGFE SRVAAAGGEN FLASECVSCG ACVQTCPTAT LTEKSLVQLG
QPERSVITTC AYCGVGCSFR AEIKGDQLVR MVPDKNGGAN HGHACVKGRF AWGYATHPDR
ITKPMIRKRL EDPWQEVSWD EAVTYAASEF RRIQLKYGRD SIGGITSSRC TNEEAYLVQK
LVRTAFGNNN VDTCARVCHS PTGYGLKQTL GESAGTQSFD SVMQADVVLV IGANPTDAHP
VFGSQLKRRL RQGARLIVID PRRIDLVDSP HARADLHLQL RPGTNVAMLN ALAHVIVTEG
LLAQSFIDAR CETGDFARWR DFVSLPDNAP EVLGPVCGVP AEQIRAAARL YATGGNAAIY
YGLGVTEHSQ GSTAVMGIAN LAMATGNIGR EGVGVNPLRG QNNVQGSCDM GSFPHELPGY
RHVSNEGVRA EFEQAWGVTL QPDPGLRIPN MFEAALDGSF KALYCQGEDI AQSDPNTQHV
TAALLAMECV VVQDIFLNET AKFAHVFLPG SSFLEKDGTF TNAERRISRV RKVMEPLAGK
ADWEATVALA NALGYPMNYR HPSEIMDEIA RLTPTFRRIS YAELDRHGSL QWPCNDAAPD
GTPTMHIDQF VRGKGRFMLT GYVPTDEKVN NRYPLLLTTG RILSQYNVGA QTRRTGNVAW
HDADRLEIHP TDAESRGIQD GDWVGIGSRA GQTVLRAKVS TRVAPGVVYT TFHFPESGAN
VITTDNSDWA TNCPEYKVTA VEVVKVFQPS QWQKRYQDFS DEQQRLLKER RTAEKAEVRR
//
