HPGT_AMYOR
ID HPGT_AMYOR Reviewed; 438 AA.
AC O52815;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=(S)-3,5-dihydroxyphenylglycine transaminase;
DE EC=2.6.1.103;
DE AltName: Full=p-hydroxyphenylglycine transaminase;
GN Name=hpgT;
OS Amycolatopsis orientalis (Nocardia orientalis).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Amycolatopsis.
OX NCBI_TaxID=31958;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RX PubMed=9545426; DOI=10.1016/s1074-5521(98)90060-6;
RA van Wageningen A., Kirkpatrick P., Williams D., Harris B., Kershaw J.,
RA Lennard N., Jones M., Jones S., Solenberg P.;
RT "Sequencing and analysis of genes involved in the biosynthesis of a
RT vancomycin group antibiotic.";
RL Chem. Biol. 5:155-162(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=11137816; DOI=10.1016/s1074-5521(00)00043-0;
RA Hubbard B.K., Thomas M.G., Walsh C.T.;
RT "Biosynthesis of L-p-hydroxyphenylglycine, a non-proteinogenic amino acid
RT constituent of peptide antibiotics.";
RL Chem. Biol. 7:931-942(2000).
CC -!- FUNCTION: Catalyzes the transamination of p-hydroxybenzoylformate to L-
CC p-hydroxyphenylglycine as part of the biosynthesis of the (S)-3,5-
CC dihydroxyphenylglycine constituent of the glycopeptide antibiotic
CC chloroeremomycin, a member of the vancomycin group of antibiotics.
CC {ECO:0000269|PubMed:11137816}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-3,5-dihydroxyphenylglycine + 2-oxoglutarate = 2-(3,5-
CC dihydroxyphenyl)-2-oxoacetate + L-glutamate; Xref=Rhea:RHEA:38347,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:75204,
CC ChEBI:CHEBI:75210; EC=2.6.1.103;
CC Evidence={ECO:0000269|PubMed:11137816};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:11137816};
CC -!- PATHWAY: Antibiotic biosynthesis; vancomycin biosynthesis.
CC {ECO:0000269|PubMed:9545426}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AJ223998; CAA11790.1; -; Genomic_DNA.
DR PIR; T30600; T30600.
DR AlphaFoldDB; O52815; -.
DR SMR; O52815; -.
DR STRING; 31958.SD37_33665; -.
DR BRENDA; 2.6.1.B17; 315.
DR UniPathway; UPA00162; -.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IDA:UniProtKB.
DR GO; GO:0033072; P:vancomycin biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Antibiotic biosynthesis; Pyridoxal phosphate;
KW Transferase.
FT CHAIN 1..438
FT /note="(S)-3,5-dihydroxyphenylglycine transaminase"
FT /id="PRO_0000430442"
FT MOD_RES 266
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 438 AA; 47777 MW; AD4C89C8B6938BF7 CRC64;
MEILVFMDSY GLSTQLSMET LHGSLTDPAI SSMNLLNELI DEYPVAISMA AGRPYEEFFD
VRLIHEYIDA YCDHLRHDRK LAEAVVTRTL FQYGTTKGII ADLIARNLAE DENIDAAAES
VVVTVGAQEA MFLILRTLRA DERDVLLAPA PTYVGLTGAA LLTDTPVWPV QSTANGVDPE
DLVLQLKRAD EQGKRVRACY VTPNFANPTG TSMDLPARHR LLEVAEANGI LLLEDNAYGL
FGSERLPSLK SLDRSGNVVY IGSFAKTGMP GARVGYVVAD QRVAGGGLLA DQLSKLKGML
TVNTSPIAQA VIAGKLLLND FSLTKANARE IAIYQRNLQL TLSELERTLG GLPEVGWNTP
TGGFFVTVTV PFVVDDELLA HAARDHGVLF TPMHHFYGGK DGFNQLRLSI SLLTPELIKE
GVTRLAALIT ARLRWPRA
