ID S5TGD1_9CORY Unreviewed; 340 AA.
AC S5TGD1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=B841_01250 {ECO:0000313|EMBL:AGS33733.1};
OS Corynebacterium maris DSM 45190.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1224163 {ECO:0000313|EMBL:AGS33733.1, ECO:0000313|Proteomes:UP000015388};
RN [1] {ECO:0000313|EMBL:AGS33733.1, ECO:0000313|Proteomes:UP000015388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Coryn-1 {ECO:0000313|Proteomes:UP000015388};
RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT "The complete genome sequence of Corynebacterium maris Coryn-1 (=DSM
RT 45190).";
RL Submitted (NOV-2012) 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; CP003924; AGS33733.1; -; Genomic_DNA.
DR RefSeq; WP_020933668.1; NC_021915.1.
DR AlphaFoldDB; S5TGD1; -.
DR STRING; 1224163.B841_01250; -.
DR KEGG; cmd:B841_01250; -.
DR PATRIC; fig|1224163.3.peg.252; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_3_11; -.
DR OrthoDB; 9809616at2; -.
DR Proteomes; UP000015388; 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}; Reference proteome {ECO:0000313|Proteomes:UP000015388};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01513, ECO:0000313|EMBL:AGS33733.1}.
FT DOMAIN 22..333
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 213
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01513"
SQ SEQUENCE 340 AA; 35834 MW; 1C90BE68D1C813CB CRC64;
MIRADLDSIP AYVPGARNDA ALKVSSNETA VAPLPSAARA MAEAAAGANR YPDMGAVELK
AALAEHLGLT PEQVAVGNGS SALCQQLAQI TCTPGDEIIF PWRSFEAYPI FARIVGATPV
AVDLLADGRH DLDAMADAIT ERTRLIFLCN PNNPSGQTLT QGEFDEFMAK VSADVVVGLD
EAYFEYNRAE DTPVATEAIA EHPNVVGLRT FSKAYGLAGV RAGYAFGSPE LMQALDKVAI
PFAVSSVAQA GAIASLAAAD ELMERTEETV AVRDTVADEL GALRSEANFV WLPGVDAQQV
AAAMAEQNVL VRAFPEGVRV TVTTEDEAQR VIAAWRAAGL
//
