PATR_MYCMM
ID PATR_MYCMM Reviewed; 361 AA.
AC B2HLJ8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Putative phenylalanine aminotransferase {ECO:0000255|HAMAP-Rule:MF_01513};
DE EC=2.6.1.- {ECO:0000255|HAMAP-Rule:MF_01513};
GN Name=pat {ECO:0000255|HAMAP-Rule:MF_01513}; OrderedLocusNames=MMAR_5326;
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=216594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M;
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
CC -!- FUNCTION: May catalyze the transamination reaction in phenylalanine
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01513}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01513};
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000255|HAMAP-Rule:MF_01513}.
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DR EMBL; CP000854; ACC43730.1; -; Genomic_DNA.
DR RefSeq; WP_012396831.1; NC_010612.1.
DR AlphaFoldDB; B2HLJ8; -.
DR SMR; B2HLJ8; -.
DR STRING; 216594.MMAR_5326; -.
DR EnsemblBacteria; ACC43730; ACC43730; MMAR_5326.
DR KEGG; mmi:MMAR_5326; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_3_11; -.
DR OMA; YPDMACT; -.
DR OrthoDB; 1248286at2; -.
DR Proteomes; UP000001190; 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 Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..361
FT /note="Putative phenylalanine aminotransferase"
FT /id="PRO_1000146151"
FT MOD_RES 221
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01513"
SQ SEQUENCE 361 AA; 38523 MW; 8D5F4DA7697BF0C3 CRC64;
MTARLRPVLA GLPVYVPGKT VPGAIKLASN ETVFGPLPSV RAAIEHATQS INRYPDNGCL
AVKAALARHV SSLSAADFGP EHIAVGCGSV SLCQQLVQIT ASVGDEVIFG WRSFELYPPQ
VQVAGATAIQ VPLTNHTFDL EAMLAAVTER TRLIIVCNPN NPTSTVVQPE ALAEFVRSVP
PHILVAIDEA YVEYLRDGTV PDSPHLVRTH SNVVVLRTFS KAYGLAGLRV GYAVGQPDVI
AALDKVYVPF TVSSLAQAAA IASVQAADEL LARTDAVVAE RGRVSAELRA AGFTVPPSQA
NFVWLPLEDR TTDFVTQAAK AHIVVRPYGA DGVRVTIAAP EENDALLRFA RCWITHRDGA
R