ID A0A0J7IQE8_9FLAO Unreviewed; 341 AA.
AC A0A0J7IQE8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=ACM39_07500 {ECO:0000313|EMBL:KMQ68358.1};
OS Chryseobacterium sp. FH2.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1674291 {ECO:0000313|EMBL:KMQ68358.1, ECO:0000313|Proteomes:UP000036315};
RN [1] {ECO:0000313|EMBL:KMQ68358.1, ECO:0000313|Proteomes:UP000036315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FH2 {ECO:0000313|EMBL:KMQ68358.1,
RC ECO:0000313|Proteomes:UP000036315};
RA Stropko S.J., Miller J.R., Newman J.D.;
RL Submitted (JUN-2015) 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; Evidence={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:KMQ68358.1}.
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DR EMBL; LFNE01000004; KMQ68358.1; -; Genomic_DNA.
DR RefSeq; WP_048510424.1; NZ_LFNE01000004.1.
DR AlphaFoldDB; A0A0J7IQE8; -.
DR STRING; 1674291.ACM39_07500; -.
DR PATRIC; fig|1674291.3.peg.1566; -.
DR OrthoDB; 9813612at2; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000036315; 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; 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; PTHR42885:SF2; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42885; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED; 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|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01023};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000313|EMBL:KMQ68358.1}.
FT DOMAIN 27..336
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 205
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01023"
SQ SEQUENCE 341 AA; 39146 MW; F586E827273D5A50 CRC64;
MTTININTLV RKNILALQPY ISFRDNNKFD SPVLLDANEN PFGKYNRYPD STQKKLKEKL
SQIKNIQPSQ IAVGNGSDEL IDLIIKVFCE PQKDSILMMN PSFAMYGFYA SINENKVIKL
NLNENFDINK DDFLKITADN SLKIFFLCSP NNPTGNCIQD IEFFIKNFNG IVVVDEAYIE
FSDEKSSVEL IERYPNLIVL QTFSKAWGKA GARVGIACSS EEIIRLINLV KAPYNVNSMS
QEMILNCLDN PNEFDKNLEN IFKERTWLNS KFEDVNCIKK VFPTDANFFL IEFEDVEKVY
ENLVENEILT SKRAPSIPNC IRINIGNQEE NQKLINILKN I
//
