DAVT_PSEPK
ID DAVT_PSEPK Reviewed; 425 AA.
AC Q88RB9; Q7BII9; Q93G46;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=5-aminovalerate aminotransferase DavT;
DE EC=2.6.1.48;
DE AltName: Full=5-aminovalerate transaminase;
DE AltName: Full=Delta-aminovalerate aminotransferase;
GN Name=davT; OrderedLocusNames=PP_0214;
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP INDUCTION, DISRUPTION PHENOTYPE, 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).
RN [2]
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).
CC -!- FUNCTION: Catalyzes the conversion of 5-aminovalerate to 5-
CC oxopentanoate. {ECO:0000269|PubMed:11679348}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 5-aminopentanoate = 5-oxopentanoate + L-
CC glutamate; Xref=Rhea:RHEA:10212, ChEBI:CHEBI:16120,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:356010;
CC EC=2.6.1.48; Evidence={ECO:0000269|PubMed:11679348};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- INDUCTION: Induced in response to corn root exudates, by lysine and by
CC 5-aminovalerate. {ECO:0000269|PubMed:11679348}.
CC -!- DISRUPTION PHENOTYPE: Mutants are impaired in lysine utilization and
CC show a slight reduction in the root colonization capacity.
CC {ECO:0000269|PubMed:11679348}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AF299291; AAK97868.1; -; Genomic_DNA.
DR EMBL; AE015451; AAN65846.1; -; Genomic_DNA.
DR RefSeq; NP_742382.1; NC_002947.4.
DR RefSeq; WP_003255866.1; NC_002947.4.
DR AlphaFoldDB; Q88RB9; -.
DR SMR; Q88RB9; -.
DR STRING; 160488.PP_0214; -.
DR EnsemblBacteria; AAN65846; AAN65846; PP_0214.
DR KEGG; ppu:PP_0214; -.
DR PATRIC; fig|160488.4.peg.228; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_6; -.
DR OMA; TSGQMSC; -.
DR PhylomeDB; Q88RB9; -.
DR BioCyc; PPUT160488:G1G01-236-MON; -.
DR BRENDA; 2.6.1.48; 5092.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
DR GO; GO:0047589; F:5-aminovalerate transaminase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
DR GO; GO:0019477; P:L-lysine catabolic process; IMP:UniProtKB.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00700; GABAtrnsam; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..425
FT /note="5-aminovalerate aminotransferase DavT"
FT /id="PRO_0000418395"
FT BINDING 112..113
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 240..243
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT MOD_RES 269
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 425 AA; 44824 MW; 6129A9C6A7837E4B CRC64;
MSKTNESLMQ RRVAAVPRGV GQIHPIFVDT AKNSTVIDVE GRELIDFAGG IAVLNTGHLH
PKVVAAVQEQ LTKVSHTCFQ VLAYEPYVEL CEKINKLVPG DFDKKTLLVT TGSEAVENAV
KIARAATGRA GVIAFTGGYH GRTMMTLGLT GKVVPYSAGM GLMPGGIFRA LFPSELHGIS
VDDAIASVER IFKNDAEPRD IAAIILEPVQ GEGGFLPAPK ELMKRLRALC DQHGILLIAD
EVQTGAGRTG TFFAMEQMGV APDLTTFAKS IAGGFPLAGV CGKAEYMDAI APGGLGGTYA
GSPIACAAAL AVIEVFEEEK LLDRSKAVGE RLTAGLREIQ KKYPIIGDVR GLGSMIAVEV
FEKGTHTPNA AAVGQVVAKA REKGLILLSC GTYGNVLRIL VPLTAEDALL DKGLAIIEEC
FAEIA
