DAVD_PSEAE
ID DAVD_PSEAE Reviewed; 483 AA.
AC Q9I6M5;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Glutarate-semialdehyde dehydrogenase {ECO:0000303|PubMed:17388807};
DE EC=1.2.1.- {ECO:0000269|PubMed:17388807};
GN Name=davD {ECO:0000250|UniProtKB:Q88RC0}; OrderedLocusNames=PA0265;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=17388807; DOI=10.1111/j.1742-4658.2007.05763.x;
RA Yamanishi Y., Mihara H., Osaki M., Muramatsu H., Esaki N., Sato T.,
RA Hizukuri Y., Goto S., Kanehisa M.;
RT "Prediction of missing enzyme genes in a bacterial metabolic network.
RT Reconstruction of the lysine-degradation pathway of Pseudomonas
RT aeruginosa.";
RL FEBS J. 274:2262-2273(2007).
CC -!- FUNCTION: Catalyzes the conversion of 5-oxopentanoate (glutarate
CC semialdehyde) to glutarate. Involved in L-lysine degradation.
CC {ECO:0000269|PubMed:17388807}.
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:0000269|PubMed:17388807};
CC -!- PATHWAY: Amino-acid degradation. {ECO:0000305|PubMed:17388807}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG03654.1; -; Genomic_DNA.
DR PIR; D83613; D83613.
DR RefSeq; NP_248956.1; NC_002516.2.
DR RefSeq; WP_003106269.1; NZ_QZGE01000035.1.
DR AlphaFoldDB; Q9I6M5; -.
DR SMR; Q9I6M5; -.
DR STRING; 287.DR97_3227; -.
DR PaxDb; Q9I6M5; -.
DR PRIDE; Q9I6M5; -.
DR EnsemblBacteria; AAG03654; AAG03654; PA0265.
DR GeneID; 881913; -.
DR KEGG; pae:PA0265; -.
DR PATRIC; fig|208964.12.peg.276; -.
DR PseudoCAP; PA0265; -.
DR HOGENOM; CLU_005391_5_1_6; -.
DR InParanoid; Q9I6M5; -.
DR OMA; IKYICMS; -.
DR PhylomeDB; Q9I6M5; -.
DR BioCyc; MetaCyc:MON-15075; -.
DR BioCyc; PAER208964:G1FZ6-267-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0047949; F:glutarate-semialdehyde dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0102810; F:glutarate-semialdehyde dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IBA:GO_Central.
DR GO; GO:0019477; P:L-lysine catabolic process; IDA:UniProtKB.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..483
FT /note="Glutarate-semialdehyde dehydrogenase"
FT /id="PRO_0000418392"
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 386
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 483 AA; 51622 MW; 1ED1643DCB83075C CRC64;
MQLKDAKLFR QQAYVDGAWV DADNGQTIKV NNPATGEIIG SVPKMGAAET RRAIEAADKA
LPAWRALTAK ERANKLRRWF DLMIENQDDL ARLMTIEQGK PLAEAKGEIA YAASFLEWFG
EEAKRIYGDT IPGHQPDKRI IVIKQPIGVT AAITPWNFPS AMITRKAGPA LAAGCTMVLK
PASQTPYSAL ALAELAERAG IPKGVFSVVT GSAGEVGGEL TSNPIVRKLT FTGSTEIGRQ
LMAECAQDIK KVSLELGGNA PFIVFDDADL DAAVEGALIS KYRNNGQTCV CANRLYVQDG
VYDAFVDKLK AAVAKLNIGN GLEAGVTTGP LIDAKAVAKV EEHIADAVSK GAKVVSGGKP
HALGGTFFEP TILVDVPKNA LVSKDETFGP LAPVFRFKDE AEVIAMSNDT EFGLASYFYA
RDLARVFRVA EQLEYGMVGI NTGLISNEVA PFGGIKASGL GREGSKYGIE DYLEIKYLCL
GGI
