APTA_CAUVC
ID APTA_CAUVC Reviewed; 439 AA.
AC Q9A3Q9;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Omega-aminotransferase {ECO:0000303|PubMed:18239415};
DE EC=2.6.1.- {ECO:0000269|PubMed:18239415};
DE AltName: Full=Beta-alanine--pyruvate aminotransferase {ECO:0000305|PubMed:18239415};
DE EC=2.6.1.18 {ECO:0000269|PubMed:18239415};
GN Name=aptA {ECO:0000303|PubMed:18239415};
GN OrderedLocusNames=CC_3143 {ECO:0000312|EMBL:AAK25105.1};
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING, AND MUTAGENESIS OF
RP VAL-227; ARG-260 AND ASN-285.
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=18239415;
RA Hwang B.Y., Ko S.H., Park H.Y., Seo J.H., Lee B.S., Kim B.G.;
RT "Identification of omega-aminotransferase from Caulobacter crescentus and
RT site-directed mutagenesis to broaden substrate specificity.";
RL J. Microbiol. Biotechnol. 18:48-54(2008).
CC -!- FUNCTION: Aminotransferase that can use beta-amino acids, aliphatic
CC amines, or aromatic amines as amino donors, and pyruvate as amino
CC acceptor. Shows high activity for short-chain beta-amino acids, with
CC the highest activity for 3-aminobutanoate and beta-alanine in vitro.
CC Displays higher activity toward aromatic amines than aliphatic amines
CC (PubMed:18239415). May be involved in beta-alanine biosynthesis and/or
CC degradation (Probable). {ECO:0000269|PubMed:18239415, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxopropanoate + L-alanine = beta-alanine + pyruvate;
CC Xref=Rhea:RHEA:14077, ChEBI:CHEBI:15361, ChEBI:CHEBI:33190,
CC ChEBI:CHEBI:57966, ChEBI:CHEBI:57972; EC=2.6.1.18;
CC Evidence={ECO:0000269|PubMed:18239415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-aminobutanoate + pyruvate = acetoacetate + L-alanine;
CC Xref=Rhea:RHEA:64308, ChEBI:CHEBI:13705, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:150018;
CC Evidence={ECO:0000269|PubMed:18239415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzylamine + pyruvate = benzaldehyde + L-alanine;
CC Xref=Rhea:RHEA:64272, ChEBI:CHEBI:15361, ChEBI:CHEBI:17169,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:225238;
CC Evidence={ECO:0000269|PubMed:18239415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-1-phenylethylamine + pyruvate = acetophenone + L-alanine;
CC Xref=Rhea:RHEA:64280, ChEBI:CHEBI:15361, ChEBI:CHEBI:27632,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:141108;
CC Evidence={ECO:0000269|PubMed:18239415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-phenylethylamine + pyruvate = 2-phenylacetaldehyde + L-
CC alanine; Xref=Rhea:RHEA:64284, ChEBI:CHEBI:15361, ChEBI:CHEBI:16424,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:225237;
CC Evidence={ECO:0000269|PubMed:18239415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-phenylpropylamine + pyruvate = 1-phenylpropan-1-one + L-
CC alanine; Xref=Rhea:RHEA:64304, ChEBI:CHEBI:15361, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:150015, ChEBI:CHEBI:425902;
CC Evidence={ECO:0000269|PubMed:18239415};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-phenylpropylamine + pyruvate = 3-phenylpropanal + L-alanine;
CC Xref=Rhea:RHEA:64300, ChEBI:CHEBI:15361, ChEBI:CHEBI:39940,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:150861;
CC Evidence={ECO:0000269|PubMed:18239415};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:18239415};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:18239415};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:18239415};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9I700}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {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; AE005673; AAK25105.1; -; Genomic_DNA.
DR PIR; E87638; E87638.
DR RefSeq; NP_421937.1; NC_002696.2.
DR AlphaFoldDB; Q9A3Q9; -.
DR SMR; Q9A3Q9; -.
DR STRING; 190650.CC_3143; -.
DR EnsemblBacteria; AAK25105; AAK25105; CC_3143.
DR KEGG; ccr:CC_3143; -.
DR PATRIC; fig|190650.5.peg.3153; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_3_5; -.
DR OMA; PLVPYNA; -.
DR BioCyc; CAULO:CC3143-MON; -.
DR Proteomes; UP000001816; Chromosome.
DR GO; GO:0016223; F:beta-alanine-pyruvate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
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 PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Pyridoxal phosphate; Pyruvate; Reference proteome;
KW Transferase.
FT CHAIN 1..439
FT /note="Omega-aminotransferase"
FT /id="PRO_0000450757"
FT BINDING 112..113
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9I700"
FT BINDING 318
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9I700"
FT MOD_RES 281
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000305|PubMed:18239415"
FT MUTAGEN 227
FT /note="V->G: Decreases activity toward 3-aminobutanoate by
FT 2-fold. Increases activity toward the aromatic beta-amino
FT acid 3-amino-3-phenylpropanoate by 2-fold."
FT /evidence="ECO:0000269|PubMed:18239415"
FT MUTAGEN 260
FT /note="R->L: Decreases activity toward 3-aminobutanoate by
FT 30-fold."
FT /evidence="ECO:0000269|PubMed:18239415"
FT MUTAGEN 285
FT /note="N->A: Decreases activity toward 3-aminobutanoate by
FT 4-fold. Increases activity toward the aromatic beta-amino
FT acid 3-amino-3-phenylpropanoate by 3-fold."
FT /evidence="ECO:0000269|PubMed:18239415"
SQ SEQUENCE 439 AA; 47629 MW; 4A7E64E3E717A395 CRC64;
MPDFGANDLD AFWMPFTPNR RFKRHPRMLS SASGMWYRTP ESREVLDATS GLWCVNAGHD
RPKIREAIQK QAAEMDYAPC FNMGHPLAFQ FASRLAQITP KGLDRIFFTN SGSESVDTAL
KIALAYHRAR GKGTKTRLIG RERGYHGVGF GGISVGGIPK NRMYFGSLLT GVDHLPHTHG
LPGNTCAKGQ PENGAHLADD LERIVALHDA SNIAAVIVEP VAGSTGVLIP PKGYLERLRA
ICDKHDILLI FDEVITGFGR VGAPFAAERF GVTPDLICMA KGLTNAAVPC GAVAASGKIY
DAMMDGADAP IELFHGYTYS AHPLACAAGL ATLETYREDD LFARAAGLEG YWQDAMHSLA
DARHVVDVRN LGLVAGIELE PRPGAPTARA MEVFETCFDE GLLIRVTGDI IALSPPLILE
KDHIDRMVET IRRVLGQVD
