(data stored in SCRATCH zone)

HOGENOM: ACIF5_1_PE1000

ID   ACIF5_1_PE1000                       STANDARD;      PRT;   365 AA.
AC   ACIF5_1_PE1000; B5EPR8;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Histidinol-phosphate aminotransferase 1; EC=2.6.1
DE   9;AltName: Full=Imidazole acetol-phosphate transaminase 1;
DE   (ACIF5_1.PE1000).
GN   Name=hisC1; OrderedLocusNames=Lferr_1020;
OS   ACIDITHIOBACILLUS FERROOXIDANS ATCC 53993.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=380394;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIF5_1.PE1000.
CC       Acidithiobacillus ferrooxidans ATCC 53993 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:B5EPR8_ACIF5
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.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. Histidinol-phosphate aminotransferase
CC       subfamily.
CC   -!- GENE_FAMILY: HOG000288510 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B5EPR8; -.
DR   EMBL; CP001132; ACH83262.1; -; Genomic_DNA.
DR   RefSeq; YP_002219469.1; NC_011206.1.
DR   ProteinModelPortal; B5EPR8; -.
DR   STRING; B5EPR8; -.
DR   GeneID; 6876989; -.
DR   GenomeReviews; CP001132_GR; Lferr_1020.
DR   KEGG; afe:Lferr_1020; -.
DR   OMA; ENPLGMP; -.
DR   ProtClustDB; CLSK2407743; -.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:HAMAP.
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_major_dom.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.
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.
DR   HOGENOMDNA; ACIF5_1.PE1000; -.
KW   histidinol-phosphate aminotransferase;
KW   Amino-acid biosynthesis; Aminotransferase; Complete proteome;
KW   Histidine biosynthesis; Pyridoxal phosphate; Transferase.
SQ   SEQUENCE   365 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MCNSYLEYTA AGVSDLRPYQ PGKPLAELER ELGIRDAIKL ASNENPLGPS PLALAAVREV
     LPALAQYPEG SAPELRALLA RQLDLDPGQF IFGNGSDQVV ELAVRALAGP GTEVIVSQYA
     FAAYAIAAQA SGATVRVAPA RDYGHDLDAM ASLLNANTRL VFIANPNNPT GTYLTADALE
     TFIDSVPSHA LVVLDEAYLE LMDAADYPDG RRWLRRFGNL MLTRTFSKAY GLAGLRCGYG
     IGHPDLMAVL ERVRQPFNVN TLAQVAAHAA LTDRAHLQAT LANNRQGIVA LRDGLCNLGL
     TILPPAGNFT AFAVPGGGQR VYEALLLRGV IVRPLTPYGM PDHLRVSVGL PVENQRFLTM
     LGEVL
//

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