ID D9Q5T0_CORP1 Unreviewed; 343 AA.
AC D9Q5T0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 01-MAY-2013, entry version 19.
DE SubName: Full=Phenylalanine aminotransferase;
GN Name=aroT; Synonyms=pat; OrderedLocusNames=Cp1002_0119;
OS Corynebacterium pseudotuberculosis (strain 1002).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=679896;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1002;
RX PubMed=21533164; DOI=10.1371/journal.pone.0018551;
RA Ruiz J.C., D'Afonseca V., Silva A., Ali A., Pinto A.C., Santos A.R.,
RA Rocha A.A., Lopes D.O., Dorella F.A., Pacheco L.G., Costa M.P.,
RA Turk M.Z., Seyffert N., Moraes P.M., Soares S.C., Almeida S.S.,
RA Castro T.L., Abreu V.A., Trost E., Baumbach J., Tauch A.,
RA Schneider M.P., McCulloch J., Cerdeira L.T., Ramos R.T., Zerlotini A.,
RA Dominitini A., Resende D.M., Coser E.M., Oliveira L.M., Pedrosa A.L.,
RA Vieira C.U., Guimaraes C.T., Bartholomeu D.C., Oliveira D.M.,
RA Santos F.R., Rabelo E.M., Lobo F.P., Franco G.R., Costa A.F.,
RA Castro I.M., Dias S.R., Ferro J.A., Ortega J.M., Paiva L.V.,
RA Goulart L.R., Almeida J.F., Ferro M.I., Carneiro N.P., Falcao P.R.,
RA Grynberg P., Teixeira S.M., Brommonschenkel S., Oliveira S.C.,
RA Meyer R., Moore R.J., Miyoshi A., Oliveira G.C., Azevedo V.;
RT "Evidence for reductive genome evolution and lateral acquisition of
RT virulence functions in two Corynebacterium pseudotuberculosis
RT strains.";
RL PLoS ONE 6:E18551-E18551(2011).
CC -!- CATALYTIC ACTIVITY: L-histidinol phosphate + 2-oxoglutarate = 3-
CC (imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate.
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
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DR EMBL; CP001809; ADL20025.1; -; Genomic_DNA.
DR RefSeq; YP_005680399.1; NC_017300.1.
DR ProteinModelPortal; D9Q5T0; -.
DR EnsemblBacteria; ADL20025; ADL20025; Cp1002_0119.
DR GeneID; 12299782; -.
DR KEGG; cpk:Cp1002_0119; -.
DR PATRIC; 42893901; VBICorPse156913_0123.
DR HOGENOM; HOG000288510; -.
DR KO; K00817; -.
DR UniPathway; UPA00031; UER00012.
DR GO; GO:0008793; F:aromatic-amino-acid:2-oxoglutarate aminotransferase activity; IEA:InterPro.
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:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01023; HisC_aminotrans_2; 1; -.
DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR005861; HisP_aminotrans.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR TIGRFAMs; TIGR01141; hisC; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW Histidine biosynthesis; Pyridoxal phosphate; Transferase.
SQ SEQUENCE 343 AA; 37103 MW; 04D08E7394A2413C CRC64;
MIREDLAQIP TYVPGHHADH TLKLSSNEVA FGPLPGAAEA MAKAITTVNR YPDMGAEEIR
ERLAEHLGLD AQQVAVGCGS SALCQQLVQI SAGPGDEVIF PWRSFEAYPI FVHVTGATPV
AVPLKEGFND LDAMAAAITE NTRLIFVCNP NNPTGTLISQ DAFLAFMNKV PSNVLVALDE
AYIEYVRAED TPLATEFIHA YPNLIGLRTF SKAFGLAGIR IGYAFGSPSL IEALNKVALP
FGVNTVAQAG AIASLENLDE LMERTEEVVL NRDRVAEHVG AGHSQTNFVW IPADSRPESP
TDIAEQLHNH DVIVRAFPEG VRITVTNSEE TDRLLAAWDA SFS
//
