ID A0A1F1I9C2_9MICC Unreviewed; 377 AA.
AC A0A1F1I9C2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=HMPREF2863_00580 {ECO:0000313|EMBL:OFR88294.1};
OS Micrococcus sp. HMSC067E09.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Micrococcus.
OX NCBI_TaxID=1739367 {ECO:0000313|EMBL:OFR88294.1, ECO:0000313|Proteomes:UP000177882};
RN [1] {ECO:0000313|EMBL:OFR88294.1, ECO:0000313|Proteomes:UP000177882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC067E09 {ECO:0000313|EMBL:OFR88294.1,
RC ECO:0000313|Proteomes:UP000177882};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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}.
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:OFR88294.1}.
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DR EMBL; LTYF01000045; OFR88294.1; -; Genomic_DNA.
DR RefSeq; WP_067192297.1; NZ_KV809408.1.
DR AlphaFoldDB; A0A1F1I9C2; -.
DR STRING; 1739367.HMPREF2863_00580; -.
DR Proteomes; UP000177882; 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; 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 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.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW Rule:MF_01513}; Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01513};
KW Reference proteome {ECO:0000313|Proteomes:UP000177882};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01513, ECO:0000313|EMBL:OFR88294.1}.
FT DOMAIN 40..348
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 242
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01513"
SQ SEQUENCE 377 AA; 40634 MW; EC3D9711B42491D4 CRC64;
MTETPKPSTT VVHPNPVIDL LPPYAAGKPP AAVEGLTPYK LSSNENPYAP VPSVLDTVTA
LVAGAEGEAS ALCRYPDPLS TALRTRLAEH HGVPADDIVT GGGSLGALTQ IITAYAGPHD
DGHRDEVLFA WRSFEAYPIV VRSAGAKDVQ VPLTADHRHD LPAMLDAITE NTRVIILCTP
NNPTGPVLTT AEVEDFLAKV PEHILVVIDE AYVEFVRHDD AVQGIEMYRK HRNVAVLRTF
SKAHGLANLR VGYSIAHPEI TRHLRVVATP FAVSTVAEQA AIASLDALDE VTERVQKVVD
ERERVVAALT EAGWDIPETH ANFVWLPLGE QAADFAARAG EQALSVRAFA GEGVRVSIGE
VEANDRFIAL ARDYRKG
//
