(data stored in SCRATCH zone)

SWISSPROT: C7QHH4_CATAD

ID   C7QHH4_CATAD            Unreviewed;       356 AA.
AC   C7QHH4;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 57.
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   OrderedLocusNames=Caci_0158 {ECO:0000313|EMBL:ACU69113.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69113.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69113.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
CC   -!- FUNCTION: May catalyze the transamination reaction in
CC       phenylalanine biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01513}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01513,
CC         ECO:0000256|SAAS:SAAS00655984};
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; CP001700; ACU69113.1; -; Genomic_DNA.
DR   RefSeq; WP_012784408.1; NC_013131.1.
DR   ProteinModelPortal; C7QHH4; -.
DR   STRING; 479433.Caci_0158; -.
DR   EnsemblBacteria; ACU69113; ACU69113; Caci_0158.
DR   KEGG; cai:Caci_0158; -.
DR   eggNOG; ENOG4105CIH; Bacteria.
DR   eggNOG; COG0079; LUCA.
DR   HOGENOM; HOG000288510; -.
DR   KO; K00817; -.
DR   OMA; HGFLVYR; -.
DR   OrthoDB; POG091H05S1; -.
DR   Proteomes; UP000000851; 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_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_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;
DR   PRODOM; C7QHH4.
DR   SWISS-2DPAGE; C7QHH4.
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01513,
KW   ECO:0000256|SAAS:SAAS00766461, ECO:0000313|EMBL:ACU69113.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01513,
KW   ECO:0000256|SAAS:SAAS00655949};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01513,
KW   ECO:0000256|SAAS:SAAS00766408, ECO:0000313|EMBL:ACU69113.1}.
FT   DOMAIN       31    347       Aminotran_1_2. {ECO:0000259|Pfam:
FT                                PF00155}.
FT   MOD_RES     222    222       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01513}.
SQ   SEQUENCE   356 AA;  38598 MW;  773E4826F0A6D5DE CRC64;
     MADDVQTPKL REALRGIPAY KAGKNPDASA FKLSSNENPY PPLPGVLEAV QKSAENFNRY
     PDMGCSALSS EIAERFGVPV EHVATGTGSV GVAQQLLQAT SGPGDEVIYA WRSFEAYPII
     TQISGATSVR VPLTPEEHHD LDAMAAAVTD RTRLIFVCNP NNPTGVAISE DALVRFLDRV
     PSDVLVVIDE AYREFVRDDS IPDGVDLYRD RPNVAVLRTF SKAYGLAGLR VGFAIAHEPV
     AAALRQTAVP FGVNSLAQVA AIESLRAEKL LLERCEALVQ ERTRVTEALR EQGWTVPESQ
     ANFIWLRLGE RTAEFAAKAE AAGIVVRPFA GEGARITVGE VEANDILLRV TAEFQE
//

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