DAVD_PSEPK
ID DAVD_PSEPK Reviewed; 480 AA.
AC Q88RC0; Q93G47;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Glutarate-semialdehyde dehydrogenase {ECO:0000250|UniProtKB:Q9I6M5};
DE EC=1.2.1.- {ECO:0000250|UniProtKB:Q9I6M5};
GN Name=davD {ECO:0000303|PubMed:11679348}; OrderedLocusNames=PP_0213;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
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.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 312-480, AND GENE NAME.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=11679348; DOI=10.1128/aem.67.11.5219-5224.2001;
RA Espinosa-Urgel M., Ramos J.L.;
RT "Expression of a Pseudomonas putida aminotransferase involved in lysine
RT catabolism is induced in the rhizosphere.";
RL Appl. Environ. Microbiol. 67:5219-5224(2001).
CC -!- FUNCTION: Catalyzes the conversion of 5-oxopentanoate (glutarate
CC semialdehyde) to glutarate. Involved in L-lysine degradation.
CC {ECO:0000250|UniProtKB:Q9I6M5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-oxopentanoate + H2O + NADP(+) = glutarate + 2 H(+) + NADPH;
CC Xref=Rhea:RHEA:57832, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16120, ChEBI:CHEBI:30921, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:Q9I6M5};
CC -!- PATHWAY: Amino-acid degradation. {ECO:0000250|UniProtKB:Q9I6M5}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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; AE015451; AAN65845.1; -; Genomic_DNA.
DR EMBL; AF299291; AAK97867.1; -; Genomic_DNA.
DR RefSeq; NP_742381.1; NC_002947.4.
DR RefSeq; WP_010951596.1; NC_002947.4.
DR AlphaFoldDB; Q88RC0; -.
DR SMR; Q88RC0; -.
DR STRING; 160488.PP_0213; -.
DR PRIDE; Q88RC0; -.
DR EnsemblBacteria; AAN65845; AAN65845; PP_0213.
DR KEGG; ppu:PP_0213; -.
DR PATRIC; fig|160488.4.peg.227; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_5_1_6; -.
DR OMA; WHRLILE; -.
DR PhylomeDB; Q88RC0; -.
DR BioCyc; PPUT160488:G1G01-234-MON; -.
DR BRENDA; 1.2.1.20; 5092.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0047949; F:glutarate-semialdehyde dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR GO; GO:0102810; F:glutarate-semialdehyde dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IEA:InterPro.
DR GO; GO:0019477; P:L-lysine catabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR010102; Succ_semiAld_DH.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01780; SSADH; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..480
FT /note="Glutarate-semialdehyde dehydrogenase"
FT /id="PRO_0000418393"
FT ACT_SITE 255
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 289
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 156..157
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 180..183
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 233..234
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 480 AA; 51549 MW; DCE4B8ECBDF1B144 CRC64;
MQLKDAQLFR QQAYINGEWL DADNGQTIKV TNPATGEVIG TVPKMGTAET RRAIEAADKA
LPAWRALTAK ERSAKLRRWF ELMIENQDDL ARLMTTEQGK PLAEAKGEIA YAASFIEWFA
EEAKRIYGDT IPGHQPDKRL IVIKQPIGVT AAITPWNFPA AMITRKAGPA LAAGCTMVLK
PASQTPYSAL ALVELAHRAG IPAGVLSVVT GSAGEVGGEL TGNSLVRKLS FTGSTEIGRQ
LMEECAKDIK KVSLELGGNA PFIVFDDADL DKAVEGAIIS KYRNNGQTCV CANRIYVQDG
VYDAFAEKLA AAVAKLKIGN GLEEGTTTGP LIDGKAVAKV QEHIEDAVSK GAKVLSGGKL
IEGNFFEPTI LVDVPKTAAV AKEETFGPLA PLFRFKDEAE VIAMSNDTEF GLASYFYARD
MSRVFRVAEA LEYGMVGINT GLISNEVAPF GGIKASGLGR EGSKYGIEDY LEIKYLCISV
