ID A0A0G3ISP2_9MYCO Unreviewed; 356 AA.
AC A0A0G3ISP2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=AB431_27885 {ECO:0000313|EMBL:AKK29869.1};
OS Mycobacterium sp. EPa45.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1545728 {ECO:0000313|EMBL:AKK29869.1, ECO:0000313|Proteomes:UP000035237};
RN [1] {ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|Proteomes:UP000035237};
RA Kato H., Ogawa N., Ohtsubo Y., Ohshima K., Toyoda A., Yamazoe A., Mori H.,
RA Maruyama F., Nagata Y., Hattori M., Fujiyama A., Kurokawa K., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45, Isolated from a Phenanthrene-Degrading Consortium.";
RL Genome Announc.0:0-0(2015).
RN [2] {ECO:0000313|EMBL:AKK29869.1, ECO:0000313|Proteomes:UP000035237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPa45 {ECO:0000313|EMBL:AKK29869.1,
RC ECO:0000313|Proteomes:UP000035237};
RX PubMed=26184940;
RA Kato H., Ogawa N., Ohtsubo Y., Oshima K., Toyoda A., Mori H., Nagata Y.,
RA Kurokawa K., Hattori M., Fujiyama A., Tsuda M.;
RT "Complete Genome Sequence of a Phenanthrene Degrader, Mycobacterium sp.
RT Strain EPa45 (NBRC 110737), Isolated from a Phenanthrene-Degrading
RT Consortium.";
RL Genome Announc. 3:e00782-15(2015).
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; CP011773; AKK29869.1; -; Genomic_DNA.
DR RefSeq; WP_047332678.1; NZ_CP011773.1.
DR AlphaFoldDB; A0A0G3ISP2; -.
DR STRING; 1545728.AB431_27885; -.
DR KEGG; mye:AB431_27885; -.
DR PATRIC; fig|1545728.4.peg.5661; -.
DR OrthoDB; 9809616at2; -.
DR Proteomes; UP000035237; Chromosome.
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:AKK29869.1}.
FT DOMAIN 25..344
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 219
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01513"
SQ SEQUENCE 356 AA; 38103 MW; B58086BD96E30B29 CRC64;
MTARLRPELA DLPAYAPGKT VQGAIKLASN ETVHGPLPGV RAAIAASAET INRYPDNGYV
ELKGHLAKHL DKDGPFAPEN IAVGCGSVSL CQQLIQITSS VGDEVVFGWR SFEIYPLQVR
VAGATAVQVP LRDYTFDLDA MLAAITDRTR LIFICNPNNP TSTVVDPEDL ARFVAAVPSD
ILIAIDEAYV EYIRDGMLPD SLGLIRSHPN VVVLRTFSKA YGLAGLRVGY AVGDPDVITA
LGKVYVPFSA TTVSQAAAIA SLSAADELLA RTDTVVAERR RVCAALTALG YTFPPSQANF
VWLPMTPEQT PDFVEQAADA RVLVRPYGTD GVRVTIGAAE ENDAFLAFAG KWIATR
//
