ID G9YJ59_9FIRM Unreviewed; 357 AA.
AC G9YJ59;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=HMPREF0080_01703 {ECO:0000313|EMBL:EHM38767.1};
OS Anaeroglobus geminatus F0357.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Anaeroglobus.
OX NCBI_TaxID=861450 {ECO:0000313|EMBL:EHM38767.1, ECO:0000313|Proteomes:UP000005481};
RN [1] {ECO:0000313|EMBL:EHM38767.1, ECO:0000313|Proteomes:UP000005481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0357 {ECO:0000313|EMBL:EHM38767.1,
RC ECO:0000313|Proteomes:UP000005481};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) 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:EHM38767.1}.
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DR EMBL; AGCJ01000075; EHM38767.1; -; Genomic_DNA.
DR RefSeq; WP_006790670.1; NZ_JH417605.1.
DR AlphaFoldDB; G9YJ59; -.
DR STRING; 861450.HMPREF0080_01703; -.
DR GeneID; 85019840; -.
DR PATRIC; fig|861450.3.peg.1573; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_1_9; -.
DR OrthoDB; 9813612at2; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000005481; 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; 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.
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:UP000005481};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01023}.
FT DOMAIN 57..350
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT MOD_RES 216
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01023"
SQ SEQUENCE 357 AA; 39679 MW; 0C9849653A1F067E CRC64;
MDNRWIRKTL QKAEPYVVPA ISESIVINAN ESPYTIFDFP EVRRDYEKRF VRFRSCRYPD
PYAEELRLAL SGYMGCEPGE ILVGNGGDEI IGLTVNTFIN PGDTVLTHWP TFDMYGIDAV
MIGGREVRVP DEDGFVRNAA AYRRKVEEVQ PKLTVICNPN NPTGHVWSLA EVESIAAAAK
NPLLVDEAYM EFAAADSAVS LIHKYDNLIV LRTLSKSFGL AGYRIGYAVA NKEMIKALSL
MKPAYNVNAM SQLVGLVAMD NRDKILAYTI PRITAARRYL AEKLRTLPDV AVYDSAANFI
LIRVPDGAAA VNALSAADIA VRSYKTEALK NCLRLTVTTN ETADRIITAL RKEYSHA
//
