ID A3P032_BURP0 Unreviewed; 356 AA.
AC A3P032;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000256|HAMAP-Rule:MF_01023};
DE EC=2.6.1.9 {ECO:0000256|HAMAP-Rule:MF_01023};
DE AltName: Full=Imidazole acetol-phosphate transaminase {ECO:0000256|HAMAP-Rule:MF_01023};
GN Name=hisC {ECO:0000256|HAMAP-Rule:MF_01023,
GN ECO:0000313|EMBL:ABN89533.1};
GN OrderedLocusNames=BURPS1106A_3723 {ECO:0000313|EMBL:ABN89533.1};
OS Burkholderia pseudomallei (strain 1106a).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=357348 {ECO:0000313|EMBL:ABN89533.1, ECO:0000313|Proteomes:UP000006738};
RN [1] {ECO:0000313|EMBL:ABN89533.1, ECO:0000313|Proteomes:UP000006738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1106a {ECO:0000313|EMBL:ABN89533.1,
RC ECO:0000313|Proteomes:UP000006738};
RA DeShazer D., Woods D.E., Nierman W.C.;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00001045, ECO:0000256|HAMAP-
CC Rule:MF_01023};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|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:0000256|ARBA:ARBA00005011, ECO:0000256|HAMAP-Rule:MF_01023}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01023}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily. {ECO:0000256|ARBA:ARBA00007970, ECO:0000256|HAMAP-
CC Rule:MF_01023}.
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DR EMBL; CP000572; ABN89533.1; -; Genomic_DNA.
DR RefSeq; WP_004199913.1; NC_009076.1.
DR AlphaFoldDB; A3P032; -.
DR SMR; A3P032; -.
DR GeneID; 56594090; -.
DR KEGG; bpl:BURPS1106A_3723; -.
DR HOGENOM; CLU_017584_3_1_4; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000006738; Chromosome I.
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 CDD; cd00609; AAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 NCBIfam; TIGR01141; hisC; 1.
DR PANTHER; PTHR43643:SF6; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43643; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE 2; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01023};
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW Rule:MF_01023}; Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01023};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01023};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000313|EMBL:ABN89533.1}.
FT DOMAIN 27..351
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 217
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01023"
SQ SEQUENCE 356 AA; 38142 MW; 6F985612DA171FE7 CRC64;
MTTPEDIIRR DVLAMTGYPV PDATGFVKLD AMENPYSLPA PLAAELGERL AHVALNRYPA
PRPAALIDRL RAVTGVPAAC DVLLGNGSDE IISMLAMACA KPGAKVLAPV PGFVMYELSA
KFAQLEFVGV PLRADLTLDI DAMLAALAEH RPALVYLAYP NNPTGTLYPD EDVERIIAAA
AASLVVIDEA YQPFAQRSWL PRAAQFDNVV VMRTMSKLGL AGIRLGYLVG LPAWLVQFDK
VRPPYNVNVL TQAAAEFLLE RVDVLDAQAA QLRDARTALA HAIGALPGAT VFPSAGNFLL
VRVPDAAAVF DVLLTERVLI KNVSKMHPLL ANCVRVTVGS PEENARLLAA LKLALP
//
