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Database: UniProt
Entry: A0A101E9S5_9FIRM
LinkDB: A0A101E9S5_9FIRM
Original site: A0A101E9S5_9FIRM 
ID   A0A101E9S5_9FIRM        Unreviewed;       367 AA.
AC   A0A101E9S5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=XD50_0468 {ECO:0000313|EMBL:KUK11212.1};
OS   Clostridia bacterium 41_269.
OC   Bacteria; Bacillota; Clostridia.
OX   NCBI_TaxID=1635275 {ECO:0000313|EMBL:KUK11212.1, ECO:0000313|Proteomes:UP000053409};
RN   [1] {ECO:0000313|Proteomes:UP000053409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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|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:KUK11212.1}.
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DR   EMBL; LGEZ01000004; KUK11212.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101E9S5; -.
DR   STRING; 1635275.XD50_0468; -.
DR   PATRIC; fig|1635275.3.peg.1618; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000053409; 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; 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.
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:KUK11212.1}.
FT   DOMAIN          35..361
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   MOD_RES         228
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   367 AA;  41615 MW;  B3F39EDF8DED1906 CRC64;
     MVFKKPICRQ EILDIKPYVP GKPIEEVERE FGIKQVIKLA SNENPLGPSP KAVEALKSKI
     KDIYMYPDGS CYYLKGAIAQ KLGAEEENIL VGNGSDEIIK LISEAYLYPG DEVIIPKPSF
     SEYEFGAKVM GGKCVFSPLK DFRIDLFDML EKLTSKTKMI YVCNPNNPTG TIVYREEVEQ
     FLNEVPDHIL VIFDEAYYEY VTDSHYPQTV NYVLEGRPNV VVLRTFSKIY GLAGLRVGYA
     VGPSSVIADV DRVREPFNVN MLAQAAAVAA LEDEEHVKRS FEINNEGKSF LYDKFEKLGI
     KYWPTEANFI WADIGKNVKE VFQEMLRKGV IIRTGDIFGY NTFVRITIGT PEQNKRLIEV
     LEEVLLA
//
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