ID A0A263D6R1_9PSEU Unreviewed; 354 AA.
AC A0A263D6R1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Putative phenylalanine aminotransferase {ECO:0000256|HAMAP-Rule:MF_01513};
DE EC=2.6.1.- {ECO:0000256|HAMAP-Rule:MF_01513};
GN Name=hisC {ECO:0000313|EMBL:OZM73267.1};
GN Synonyms=pat {ECO:0000256|HAMAP-Rule:MF_01513};
GN ORFNames=CFN78_10410 {ECO:0000313|EMBL:OZM73267.1};
OS Amycolatopsis antarctica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1854586 {ECO:0000313|EMBL:OZM73267.1, ECO:0000313|Proteomes:UP000242444};
RN [1] {ECO:0000313|EMBL:OZM73267.1, ECO:0000313|Proteomes:UP000242444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU-G6 {ECO:0000313|EMBL:OZM73267.1,
RC ECO:0000313|Proteomes:UP000242444};
RA Wang J., Leiva S., Huang J., Huang Y.;
RT "Amycolatopsis antarcticus sp. nov., isolated from the surface of an
RT Antarcticus brown macroalga.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May catalyze the transamination reaction in phenylalanine
CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01513}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01513};
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|HAMAP-Rule:MF_01513}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZM73267.1}.
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DR EMBL; NKYE01000005; OZM73267.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A263D6R1; -.
DR InParanoid; A0A263D6R1; -.
DR OrthoDB; 9809616at2; -.
DR Proteomes; UP000242444; Unassembled WGS sequence.
DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR HAMAP; MF_01513; Phe_aminotrans_2; 1.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR005861; HisP_aminotrans.
DR InterPro; IPR024892; Pat.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01141; hisC; 1.
DR PANTHER; PTHR43643; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE 2; 1.
DR PANTHER; PTHR43643:SF3; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE 2; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW Rule:MF_01513};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01513}; Reference proteome {ECO:0000313|Proteomes:UP000242444};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01513}.
FT DOMAIN 31..350
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 222
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01513"
SQ SEQUENCE 354 AA; 37941 MW; 91E4ADFFC975D591 CRC64;
MTSRPDGAVH TRADLDSLPN YVPGRSVPGA VKLASNEVPG GPLPSVAEAI AEAAAQVNRY
PDMGASALID RLARELDVPA EQVSVGCGSV SVCLQLVQAI CDPGDEVLFA WRSFEAYPIL
TRVAGATQVT VPLDDDHTHD LDAMLAAITP RTRVVFVCNP NNPTGTAVRR EELERFLDAV
PSHVLVALDE AYREFVSDEE VPDGVDLARG RSNVAVLRTF SKAYGLAGLR IGYAYAPAQV
TAALRKVFVP FSVNALAQAA AIASLDAKAE LLERCAEIVV ERDRVREALL AAGFEVPRTQ
ANFVWLPLGE RAVAFAEHAL EHKLVVRPFA GDGVRVTIGT AEENDRLIEA ARAF
//
