ID A0A0S4KQI1_9BACT Unreviewed; 361 AA.
AC A0A0S4KQI1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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:CUQ66261.1};
GN ORFNames=NITINOP_1286 {ECO:0000313|EMBL:CUQ66261.1};
OS Candidatus Nitrospira inopinata.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1715989 {ECO:0000313|EMBL:CUQ66261.1, ECO:0000313|Proteomes:UP000066284};
RN [1] {ECO:0000313|Proteomes:UP000066284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Daims H.;
RL Submitted (SEP-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|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|HAMAP-Rule:MF_01023}.
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DR EMBL; LN885086; CUQ66261.1; -; Genomic_DNA.
DR RefSeq; WP_062484188.1; NZ_LN885086.1.
DR AlphaFoldDB; A0A0S4KQI1; -.
DR STRING; 1715989.NITINOP_1286; -.
DR KEGG; nio:NITINOP_1286; -.
DR OrthoDB; 9813612at2; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000066284; Chromosome 1.
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:SF3; 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 Reference proteome {ECO:0000313|Proteomes:UP000066284};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01023, ECO:0000313|EMBL:CUQ66261.1}.
FT DOMAIN 32..346
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 224
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01023"
SQ SEQUENCE 361 AA; 39472 MW; D117B985728BAC57 CRC64;
MALYIHPDIR SLTPYVPGKP IEELQRELGL DRVIKLASNE NPIGPSSRAL AALAGATDNL
HRYPDGGGHR LRQVLAERWK VSSEQIIVGN GSDELLGLLA RAFLAPGDDA VMADHTFVIY
RMEVTAAHGN PIVVPLTNWT HDLDAMARAV TPRTRLLFVC NPNNPTGTMV SAEEVERLMA
SVPNDVVVVF DEAYFEYVRD PRFPDTIAYV RDGRNAVVLR TFSKIYGLAG LRIGYGITTP
EIAGILNRIR PPFNANSLAQ RAAAAALGDE EHVARSRSVN AEGMAQVSQG LEALGLTPIP
SQTNFLYFDV GRDGRQVFEA LLREGIIVRH IEGTMLRVTI GLADENAAFL QALKRVLACE
T
//