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Database: UniProt/TrEMBL
Entry: D9Q5T0_CORP1
LinkDB: D9Q5T0_CORP1
Original site: D9Q5T0_CORP1 
ID   D9Q5T0_CORP1            Unreviewed;       343 AA.
AC   D9Q5T0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   26-NOV-2014, entry version 30.
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   ECO:0000313|EMBL:ADL20025.1};
GN   OrderedLocusNames=Cp1002_0119 {ECO:0000313|EMBL:ADL20025.1};
OS   Corynebacterium pseudotuberculosis (strain 1002).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=679896 {ECO:0000313|EMBL:ADL20025.1, ECO:0000313|Proteomes:UP000008684};
RN   [1] {ECO:0000313|EMBL:ADL20025.1, ECO:0000313|Proteomes:UP000008684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1002 {ECO:0000313|EMBL:ADL20025.1,
RC   ECO:0000313|Proteomes:UP000008684};
RX   PubMed=21037006; DOI=10.1128/JB.01211-10;
RG   Consortium: Rede Paraense de Genomica e Proteomica (RPGP);
RA   Silva A., Schneider M.P., Cerdeira L., Barbosa M.S., Ramos R.T.,
RA   Carneiro A.R., Santos R., Lima M., D'Afonseca V., Almeida S.S.,
RA   Santos A.R., Soares S.C., Pinto A.C., Ali A., Dorella F.A., Rocha F.,
RA   de Abreu V.A., Trost E., Tauch A., Shpigel N., Miyoshi A., Azevedo V.;
RT   "Complete genome sequence of Corynebacterium pseudotuberculosis I19, a
RT   strain isolated from a cow in Israel with bovine mastitis.";
RL   J. Bacteriol. 193:323-324(2011).
RN   [2] {ECO:0000313|EMBL:ADL20025.1, ECO:0000313|Proteomes:UP000008684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1002 {ECO:0000313|EMBL:ADL20025.1,
RC   ECO:0000313|Proteomes:UP000008684};
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   -!- FUNCTION: May catalyze the transamination reaction in
CC       phenylalanine biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01513}.
CC   -!- COFACTOR:
CC       Note=Pyridoxal phosphate. {ECO:0000256|HAMAP-Rule:MF_01513,
CC       ECO:0000256|SAAS:SAAS00112214};
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; 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   BioCyc; CPSE679896:GLBP-131-MONOMER; -.
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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01141; hisC; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01513,
KW   ECO:0000256|SAAS:SAAS00112504};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008684};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01513,
KW   ECO:0000256|SAAS:SAAS00111961};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01513,
KW   ECO:0000256|SAAS:SAAS00112142}.
FT   MOD_RES     212    212       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01513}.
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
//
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