HIS8_CLONN
ID HIS8_CLONN Reviewed; 356 AA.
AC A0PXP5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01023};
DE EC=2.6.1.9 {ECO:0000255|HAMAP-Rule:MF_01023};
DE AltName: Full=Imidazole acetol-phosphate transaminase {ECO:0000255|HAMAP-Rule:MF_01023};
GN Name=hisC {ECO:0000255|HAMAP-Rule:MF_01023}; OrderedLocusNames=NT01CX_1063;
OS Clostridium novyi (strain NT).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=386415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NT;
RX PubMed=17115055; DOI=10.1038/nbt1256;
RA Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA Zhou S.;
RT "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT NT.";
RL Nat. Biotechnol. 24:1573-1580(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-
CC oxopropyl phosphate + L-glutamate; Xref=Rhea:RHEA:23744,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57766,
CC ChEBI:CHEBI:57980; EC=2.6.1.9; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01023};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01023};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC {ECO:0000255|HAMAP-Rule:MF_01023}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01023}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01023}.
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DR EMBL; CP000382; ABK61580.1; -; Genomic_DNA.
DR RefSeq; WP_011721167.1; NC_008593.1.
DR AlphaFoldDB; A0PXP5; -.
DR SMR; A0PXP5; -.
DR STRING; 386415.NT01CX_1063; -.
DR EnsemblBacteria; ABK61580; ABK61580; NT01CX_1063.
DR KEGG; cno:NT01CX_1063; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_1_9; -.
DR OMA; NYHVAGF; -.
DR OrthoDB; 1248286at2; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000008220; Chromosome.
DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01023; HisC_aminotrans_2; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR005861; HisP_aminotrans.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01141; hisC; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..356
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_0000319752"
FT MOD_RES 213
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ SEQUENCE 356 AA; 41156 MW; F2480BB27E680816 CRC64;
MIQELFRKDI KDFRPYDAKG EKYKIKLDAN ESFIGLSKEI KNKIIRSLIE LEFNNYPDPD
ATKLKKAYGD YIGIDEKNIM VGNGSDELIQ ILTNAFLDKN EKIVTLNPDF SMYEVYTKVR
GGKVSVFDLD EDFKLNVNKI IEYINEEKPK MFIFSNPNNP TGGVIPKYDI IKIIENVNCI
VVVDEAYMEF YGDSILDYIK KYDNLIVLRT ASKAIGSAAL RLGFLITNDT LLREIKKVKP
PFNVNSVSQV IGEIILKDKD FIRESIDKVL YERNYLLKEL KKIDGLKVYE TKSNFVLIYN
ENANEINESL IKIGIKVRSF TDENLKNFIR ITVGSREQNI EVINCIKGDN YDYKEM
