AAT_PSEAE
ID AAT_PSEAE Reviewed; 398 AA.
AC P72173;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Aspartate aminotransferase;
DE Short=AspAT;
DE EC=2.6.1.1;
DE AltName: Full=Transaminase A;
GN Name=aspC; OrderedLocusNames=PA3139;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-75.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8808952; DOI=10.1128/jb.178.18.5550-5554.1996;
RA Rivera E., Vila L., Barbe J.;
RT "The uvrB gene of Pseudomonas aeruginosa is not DNA damage inducible.";
RL J. Bacteriol. 178:5550-5554(1996).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG06527.1; -; Genomic_DNA.
DR EMBL; X93486; CAA63758.1; -; Genomic_DNA.
DR PIR; B83252; B83252.
DR RefSeq; NP_251829.1; NC_002516.2.
DR RefSeq; WP_003104588.1; NZ_QZGE01000023.1.
DR AlphaFoldDB; P72173; -.
DR SMR; P72173; -.
DR STRING; 287.DR97_4790; -.
DR PaxDb; P72173; -.
DR PRIDE; P72173; -.
DR EnsemblBacteria; AAG06527; AAG06527; PA3139.
DR GeneID; 882671; -.
DR KEGG; pae:PA3139; -.
DR PATRIC; fig|208964.12.peg.3291; -.
DR PseudoCAP; PA3139; -.
DR HOGENOM; CLU_032440_1_2_6; -.
DR InParanoid; P72173; -.
DR OMA; VGACTIV; -.
DR PhylomeDB; P72173; -.
DR BioCyc; PAER208964:G1FZ6-3199-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0033585; P:L-phenylalanine biosynthetic process from chorismate via phenylpyruvate; IBA:GO_Central.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11879; PTHR11879; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..398
FT /note="Aspartate aminotransferase"
FT /id="PRO_0000123845"
FT BINDING 36
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT MOD_RES 248
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 398 AA; 43319 MW; 4FE1D5709BAE599F CRC64;
MSLFSAVEMA PRDPILGLNE AFNADTRPGK INLGVGVYYN EEGRIPLLRA VQAAEKARIE
AHAPRGYLPI EGIAAYDQGV QKLLFGNESE LLAAGRVVTT QAVGGTGALK LGADFLKRLL
PDATVAISDP SWENHRALFE AAGFPVQNYR YYDAASNGVN RAGLLEDLNA LPARSIVVLH
ACCHNPTGVD LELDDWKQVL DVLKAKGHVP FLDIAYQGFG NGIEEDAAAV RLFAQSGLSF
FVSSSFSKSF SLYGERVGAL SIVTESRDES ARVLSQVKRV IRTNYSNPPT HGASVVSSVL
NSPELRALWE QELGEMRDRI RDMRLAMVEQ LAAHGAKRDF SFVGRQRGMF SYSGLTADQV
ERLKTEFGIY AVSTGRICVA ALNKSNLETI TKAIVQVL
