ID C7MSF7_SACVD Unreviewed; 351 AA.
AC C7MSF7;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 01-MAY-2013, entry version 27.
DE RecName: Full=Putative phenylalanine aminotransferase;
DE EC=2.6.1.-;
GN Name=pat; OrderedLocusNames=Svir_01830;
OS Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 /
OS NBRC 12207 / P101).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Pseudonocardineae; Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=471857;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101;
RX DOI=10.4056/sigs.20263;
RA Pati A., Sikorski J., Nolan M., Lapidus A., Copeland A.,
RA Glavina del Rio T., Lucas S., Chen F., Tice H., Pitluck S.,
RA Cheng J.-F., Chertkov O., Brettin T., Han C., Detter J.C., Kuske C.,
RA Bruce D., Goodwin L., Chain P., D'haeseleer P., Chen A.,
RA Palaniappan K., Ivanova N., Mavromatis K., Mikhailova N., Rohde M.,
RA Tindall B.J., Goeker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.-P.;
RT "Complete genome sequence of Saccharomonospora viridis type strain
RT (P101).";
RL Stand. Genomic Sci. 1:141-149(2009).
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; CP001683; ACU95270.1; -; Genomic_DNA.
DR RefSeq; YP_003132097.1; NC_013159.1.
DR ProteinModelPortal; C7MSF7; -.
DR STRING; 471857.Svir_01830; -.
DR EnsemblBacteria; ACU95270; ACU95270; Svir_01830.
DR GeneID; 8385521; -.
DR KEGG; svi:Svir_01830; -.
DR PATRIC; 23390740; VBISacVir111818_0182.
DR eggNOG; COG0079; -.
DR HOGENOM; HOG000288510; -.
DR KO; K00817; -.
DR OMA; YIELADI; -.
DR ProtClustDB; CLSK2535815; -.
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_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; Complete proteome; Pyridoxal phosphate; Transferase.
FT MOD_RES 217 217 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 351 AA; 37724 MW; 9429D4893CE919DD CRC64;
MSAIPTRADL AALPAYVPGR TVPGAIKLAS NEVPEGPLPS VVDAITKAGT EINRYPDMGA
WALVDRLANE FDVPASRVAV GCGSVSLCQQ FVQALCAPGE EALFAWRSFE AYPIVTQVAG
ATPVRVPLTA SHHHDLDAML AAITPRTRLV FVCNPNNPTG TALRTEELTA FLDRVPSDVV
VVLDEAYREF VTDPDVPDGM ELARAYRNVA VLRTFSKAYG LAGLRVGYAV AAEEVIEAVR
KVYVAFSVNA VAQAAALASL DAKDELLARC DDIVRERTRV HDALRELGYA VPETLANFVW
LPLGERTNAF AEHALENKVV VRPFAGEGVR VTIGTPEEND VFLAAARSFL A
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