DAVT_PSEAE
ID DAVT_PSEAE Reviewed; 426 AA.
AC Q9I6M4;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=PA0266;
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, COFACTOR, 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-aminovalerate to 5-
CC oxopentanoate. {ECO:0000269|PubMed:17388807}.
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:17388807};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000305|PubMed:17388807};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG03655.1; -; Genomic_DNA.
DR PIR; B83611; B83611.
DR RefSeq; NP_248957.1; NC_002516.2.
DR RefSeq; WP_003106268.1; NZ_QZGE01000035.1.
DR AlphaFoldDB; Q9I6M4; -.
DR SMR; Q9I6M4; -.
DR STRING; 287.DR97_3228; -.
DR PaxDb; Q9I6M4; -.
DR PRIDE; Q9I6M4; -.
DR EnsemblBacteria; AAG03655; AAG03655; PA0266.
DR GeneID; 880917; -.
DR KEGG; pae:PA0266; -.
DR PATRIC; fig|208964.12.peg.278; -.
DR PseudoCAP; PA0266; -.
DR HOGENOM; CLU_016922_10_0_6; -.
DR InParanoid; Q9I6M4; -.
DR OMA; TSGQMSC; -.
DR PhylomeDB; Q9I6M4; -.
DR BioCyc; MetaCyc:MON-15074; -.
DR BioCyc; PAER208964:G1FZ6-268-MON; -.
DR BRENDA; 2.6.1.48; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IBA:GO_Central.
DR GO; GO:0047589; F:5-aminovalerate transaminase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; 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 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..426
FT /note="5-aminovalerate aminotransferase DavT"
FT /id="PRO_0000418394"
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 426 AA; 45220 MW; 363FC13BF7C70C55 CRC64;
MSKTNESLLK RRQAAVPRGV GQIHPVVAER AENSTVWDVE GREYIDFAGG IAVLNTGHLH
PKVIAAVQEQ LGKLSHTCFQ VLAYEPYIEL AEEIAKRVPG DFPKKTLLVT SGSEAVENAV
KIARAATGRA GVIAFTGAYH GRTMMTLGLT GKVVPYSAGM GLMPGGIFRA LAPCELHGVS
EDDSIASIER IFKNDAQPQD IAAIIIEPVQ GEGGFYVNSK SFMQRLRALC DQHGILLIAD
EVQTGAGRTG TFFATEQLGI VPDLTTFAKS VGGGFPISGV AGKAEIMDAI APGGLGGTYA
GSPIACAAAL AVLKVFEEEK LLERSQAVGE RLKAGLREIQ AKHKVIGDVR GLGSMVAIEL
FEGGDTHKPA AELVSKIVVR AREKGLILLS CGTYYNVIRF LMPVTIPDAQ LEKGLAILAE
CFDELA
