ID A0A316AZY6_9ACTN Unreviewed; 359 AA.
AC A0A316AZY6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=pat {ECO:0000256|HAMAP-Rule:MF_01513};
GN ORFNames=BXY45_102183 {ECO:0000313|EMBL:PWJ55817.1};
OS Quadrisphaera granulorum.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Quadrisphaera.
OX NCBI_TaxID=317664 {ECO:0000313|EMBL:PWJ55817.1, ECO:0000313|Proteomes:UP000245469};
RN [1] {ECO:0000313|EMBL:PWJ55817.1, ECO:0000313|Proteomes:UP000245469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44889 {ECO:0000313|EMBL:PWJ55817.1,
RC ECO:0000313|Proteomes:UP000245469};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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:PWJ55817.1}.
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DR EMBL; QGDQ01000002; PWJ55817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316AZY6; -.
DR Proteomes; UP000245469; 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:UP000245469};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01513, ECO:0000313|EMBL:PWJ55817.1}.
FT DOMAIN 28..333
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 217
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01513"
SQ SEQUENCE 359 AA; 37821 MW; F563FDBA9B2A4583 CRC64;
MRAAISALPG YVPGRPAPVA PDGTSYKISS NENPYPPLPA VLEVVQRAVT EINRYPDMAS
TQLVSALAER LDVPAPRIVT GTGSVGVLSS LLQAVCEAGD EVVFAWRSFE AYPIVVGLSG
ATAVPVPLDG AGRHDLDAMA DAITERTRLV LVCTPNNPTG PVVGAQELEA FLGRVPRDVL
VVVDEAYLEF VRDPTAADGL AVHRAHPNVM VLRTFSKAYG LAGLRVGYAV AHEPVAEALR
RAAVPFGVSS IAQLAAVASL EQEKALLERV DGIVDERERV AAELTRQGWR LPRSEANFVY
LPVGSATPDL VAACAEAGLS VRGYGSDGVR ATVGDAAADD VLLEVCGAFL QRWSPDRVG
//
