GenomeNet

Database: UniProt
Entry: A0A0S4KQI1_9BACT
LinkDB: A0A0S4KQI1_9BACT
Original site: A0A0S4KQI1_9BACT 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system