ID A0A1C4WUM7_MICEC Unreviewed; 372 AA.
AC A0A1C4WUM7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=GA0070618_2510 {ECO:0000313|EMBL:SCE99900.1};
OS Micromonospora echinospora (Micromonospora purpurea).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1877 {ECO:0000313|EMBL:SCE99900.1, ECO:0000313|Proteomes:UP000198253};
RN [1] {ECO:0000313|EMBL:SCE99900.1, ECO:0000313|Proteomes:UP000198253}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43816 {ECO:0000313|EMBL:SCE99900.1,
RC ECO:0000313|Proteomes:UP000198253};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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}.
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DR EMBL; LT607413; SCE99900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4WUM7; -.
DR InParanoid; A0A1C4WUM7; -.
DR OrthoDB; 9809616at2; -.
DR Proteomes; UP000198253; Chromosome i.
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};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01513, ECO:0000313|EMBL:SCE99900.1}.
FT DOMAIN 42..360
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 233
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01513"
SQ SEQUENCE 372 AA; 39513 MW; 36645FD64DE5AFC0 CRC64;
MTDTGRREPP IRLTRADLDA LPNYVPGRSP ADLARELGIP EAIKLASNEV PYGPLPGVVE
AIAEAAAGSH RYPDMGVVAL HSALAERYGV TPEQIVTGCG SVALAEHLVR ATCLPGDEVV
YSWRSFEAYP IVVATSGATS VPVPNLPDHG HDLAAMAAAV TDRTRMVVVC NPNNPTGTFL
RRPELERFLD AVPDDVLVVI DEAYREFVTD PEVPDGLGYV DRPNVAVLRT LSKAWGLAGM
RVGFMVAQPA VAAAVRKVVT PFSINAPAQA AALAALAQAD EVERRCALVV AERDRVTEAL
RAFVPDLPTS QGNFVWLPLG EGAITFAKAC EARGVIVRPF PGDGVRMTIG TPAENDAFLA
VVESALSKEI GR
//
