ID A0A081P8E8_9BACL Unreviewed; 355 AA.
AC A0A081P8E8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ORFNames=ET33_24010 {ECO:0000313|EMBL:KEQ26971.1};
OS Paenibacillus tyrfis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1501230 {ECO:0000313|EMBL:KEQ26971.1, ECO:0000313|Proteomes:UP000028123};
RN [1] {ECO:0000313|EMBL:KEQ26971.1, ECO:0000313|Proteomes:UP000028123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSt1 {ECO:0000313|EMBL:KEQ26971.1,
RC ECO:0000313|Proteomes:UP000028123};
RA Aw Y.K., Ong K.S., Gan H.M., Lee S.M.;
RT "Draft genome sequence of Paenibacillus sp. MSt1.";
RL Submitted (JUN-2014) 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|HAMAP-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEQ26971.1}.
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DR EMBL; JNVM01000004; KEQ26971.1; -; Genomic_DNA.
DR RefSeq; WP_036676639.1; NZ_JNVM01000004.1.
DR AlphaFoldDB; A0A081P8E8; -.
DR eggNOG; COG0079; Bacteria.
DR OrthoDB; 9813612at2; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000028123; Unassembled WGS sequence.
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; IPR001917; Aminotrans_II_pyridoxalP_BS.
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; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE 2; 1.
DR PANTHER; PTHR43643:SF3; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE 2; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 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|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01023}; Reference proteome {ECO:0000313|Proteomes:UP000028123};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000313|EMBL:KEQ26971.1}.
FT DOMAIN 27..346
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 212
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01023"
SQ SEQUENCE 355 AA; 38955 MW; 7ECB74152023FAAF CRC64;
MTLILPHIER LTPYALGDLP PEGIAAIKLN QNESPYPPSP LVLEALRTLG EEELRRYPDA
RCVQLRAALS RLHGVKDEQI FCGNGSSEII SLIVKGFVGP NRRLALPDPS FSLYHTVAAS
NQASSIAVPT RSDFTVDTEL LMNSGADAIV LVNPNAPTGH LLPLEEAERL VSRFPGLVVI
DEAYIDFADR GATAIPLVDR YPNVIVVRTF SKAYALCGAR VGYCVAAEPL IAALEKSKDI
YNINSISRKL AVAALEDREY TERTVAAVKA TRDSFIAELQ SLGFDVIPSQ TNFVLCTPPA
GAGKPDARQW YRRLLERNIY VRHFEHPRLA DKLRISIGTD EEMAAVTAVL RELLA
//
