ID   PATR_COREF              Reviewed;         342 AA.
AC   Q8FU28;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 2.
DT   01-MAY-2013, entry version 64.
DE   RecName: Full=Putative phenylalanine aminotransferase;
DE            EC=2.6.1.-;
GN   Name=pat; OrderedLocusNames=CE0193;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM
OS   11189 / NBRC 100395).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E.,
RA   Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K.,
RA   Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
CC   -!- FUNCTION: May catalyze the transamination reaction in
CC       phenylalanine biosynthesis (By similarity).
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC17003.1; Type=Erroneous initiation;
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DR   EMBL; BA000035; BAC17003.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_736803.1; NC_004369.1.
DR   ProteinModelPortal; Q8FU28; -.
DR   STRING; 196164.CE0193; -.
DR   EnsemblBacteria; BAC17003; BAC17003; BAC17003.
DR   GeneID; 1032317; -.
DR   KEGG; cef:CE0193; -.
DR   PATRIC; 21486576; VBICorEff9312_0241.
DR   HOGENOM; HOG000288510; -.
DR   KO; K00817; -.
DR   ProtClustDB; PRK03321; -.
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:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01513; Phe_aminotrans_2; 1; -.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR024892; AroT.
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   Aminotransferase; Complete proteome; Pyridoxal phosphate; Transferase.
FT   CHAIN         1    342       Putative phenylalanine aminotransferase.
FT                                /FTId=PRO_0000153511.
FT   MOD_RES     214    214       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   342 AA;  36446 MW;  34D2B6340EE6FF01 CRC64;
     MIRADLTDIP TYVPGKNLGD ALKLSSNEVA FPPLPAAVSA ITEAATGANR YPDMGAVELR
     GVLADHLELT PEQITVGCGS SALCQQLVQA TCAAGDEVIF PWRSFEAYPI FARVAGATAV
     PIPLLPDTQG HDLEGMLDAI TDRTRLIFLC NPNNPSGTTF TEEQFEAFMQ RVPADVVVGL
     DEAYFEFNRA EDSPVSTEAV QRYPNVIGLR TFSKAYGLAG VRVGYAFGNP ELIGAMNKVA
     IPFAVSSLAQ AAAIASLNAA DELLERTEEV VTERERVAQV VGAAPSQANF VWLPGEGAAE
     LAGRLAEHGV VIRAFPEGAR ITVTNAAETD RLIRAWEAVH HG
//

ID   C8NRB0_COREF            Unreviewed;       357 AA.
AC   C8NRB0;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   01-MAY-2013, entry version 30.
DE   RecName: Full=Putative phenylalanine aminotransferase;
DE            EC=2.6.1.-;
GN   Name=hisC2; Synonyms=pat; ORFNames=HMPREF0290_2535;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM
OS   11189 / NBRC 100395).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YS-314;
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z.,
RA   Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA   Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L.,
RA   Nguyen N., Okwuonu G., Ongeri F., Pham C., Simmons D.,
RA   Wilczek-Boney K., Hale W., Jakkamsetti A., Pham P., Ruth R.,
RA   San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C., Zhu D., Lee S.,
RA   Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S., Hirani K.,
RA   Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May catalyze the transamination reaction in
CC       phenylalanine biosynthesis (By similarity).
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family.
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DR   EMBL; ACLI01000105; EEW48892.1; -; Genomic_DNA.
DR   RefSeq; NP_736803.1; NC_004369.1.
DR   ProteinModelPortal; C8NRB0; -.
DR   GeneID; 1032317; -.
DR   KEGG; cef:CE0193; -.
DR   PATRIC; 21486576; VBICorEff9312_0241.
DR   eggNOG; COG0079; -.
DR   KO; K00817; -.
DR   OMA; NNTKIVW; -.
DR   ProtClustDB; PRK03321; -.
DR   BioCyc; CEFF196164:GJW8-197-MONOMER; -.
DR   GO; GO:0008793; F:aromatic-amino-acid:2-oxoglutarate aminotransferase activity; IEA:InterPro.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:EC.
DR   GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:EC.
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; IPR024892; AroT.
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   Aminotransferase; Pyridoxal phosphate; Transferase.
FT   MOD_RES     229    229       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   357 AA;  38097 MW;  C737263F74A82E49 CRC64;
     MCQTIVSTPA SRVEFMIRAD LTDIPTYVPG KNLGDALKLS SNEVAFPPLP AAVSAITEAA
     TGANRYPDMG AVELRGVLAD HLELTPEQIT VGCGSSALCQ QLVQATCAAG DEVIFPWRSF
     EAYPIFARVA GATAVPIPLL PDTQGHDLEG MLDAITDRTR LIFLCNPNNP SGTTFTEEQF
     EAFMQRVPAD VVVGLDEAYF EFNRAEDSPV STEAVQRYPN VIGLRTFSKA YGLAGVRVGY
     AFGNPELIGA MNKVAIPFAV SSLAQAAAIA SLNAADELLE RTEEVVTERE RVAQVVGAAP
     SQANFVWLPG EGAAELAGRL AEHGVVIRAF PEGARITVTN AAETDRLIRA WEAVHHG
//