PHHC_PSEAE
ID PHHC_PSEAE Reviewed; 399 AA.
AC P43336;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Aromatic-amino-acid aminotransferase;
DE EC=2.6.1.57;
GN Name=phhC; OrderedLocusNames=PA0870;
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 [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8108417; DOI=10.1073/pnas.91.4.1366;
RA Zhao G., Xia T., Song J., Roy R.A.;
RT "Pseudomonas aeruginosa possesses homologues of mammalian phenylalanine
RT hydroxylase and 4 alpha-carbinolamine dehydratase/DCoH as part of a three-
RT component gene cluster.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1366-1370(1994).
RN [2]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + an aromatic L-alpha-amino acid = an aromatic
CC oxo-acid + L-glutamate; Xref=Rhea:RHEA:17533, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:73309, ChEBI:CHEBI:84824; EC=2.6.1.57;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
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; M88627; AAA25938.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04259.1; -; Genomic_DNA.
DR PIR; D83535; D83535.
DR RefSeq; NP_249561.1; NC_002516.2.
DR RefSeq; WP_003114240.1; NZ_QZGE01000007.1.
DR AlphaFoldDB; P43336; -.
DR SMR; P43336; -.
DR STRING; 287.DR97_1073; -.
DR PaxDb; P43336; -.
DR PRIDE; P43336; -.
DR DNASU; 880839; -.
DR EnsemblBacteria; AAG04259; AAG04259; PA0870.
DR GeneID; 880839; -.
DR KEGG; pae:PA0870; -.
DR PATRIC; fig|208964.12.peg.904; -.
DR PseudoCAP; PA0870; -.
DR HOGENOM; CLU_032440_0_1_6; -.
DR InParanoid; P43336; -.
DR OMA; PTWPIHE; -.
DR PhylomeDB; P43336; -.
DR BioCyc; MetaCyc:MON-12023; -.
DR BioCyc; PAER208964:G1FZ6-885-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; IBA:GO_Central.
DR GO; GO:0080130; F:L-phenylalanine: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 GO; GO:0006572; P:tyrosine catabolic process; IMP:CACAO.
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 Amino-acid biosynthesis; Aminotransferase;
KW Aromatic amino acid biosynthesis; Cytoplasm; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..399
FT /note="Aromatic-amino-acid aminotransferase"
FT /id="PRO_0000123895"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 247
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 382
FT /note="D -> H (in Ref. 1; AAA25938)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="D -> G (in Ref. 1; AAA25938)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 43273 MW; B6162FE13EBDB6E1 CRC64;
MSHFAKVARV PGDPILGLLD AYRNDPRADK LDLGVGVYKD AQGLTPILRS VKLAEQRLVE
QETTKSYVGG HGDALFAARL AELALGAASP LLLEQRADAT QTPGGTGALR LAGDFIAHCL
PGRGIWLSDP TWPIHETLFA AAGLKVSHYP YVSADNRLDV EAMLAGLERI PQGDVVLLHA
CCHNPTGFDL SHDDWRRVLD VVRRRELLPL IDFAYQGFGD GLEEDAWAVR LFAGELPEVL
VTSSCSKNFG LYRDRVGALI VCAQNAEKLT DLRSQLAFLA RNLWSTPPAH GAEVVAAILG
DSELKGLWQE EVEGMRSRIA SLRIGLVEAL APHGLAERFA HVGAQRGMFS YTGLSPQQVA
RLRDEHAVYL VSSGRANVAG LDARRLDRLA QAIAQVCAD
