HIS8_CORGL
ID HIS8_CORGL Reviewed; 366 AA.
AC Q9KJU4;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Histidinol-phosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_01023};
DE EC=2.6.1.9 {ECO:0000255|HAMAP-Rule:MF_01023};
DE AltName: Full=Imidazole acetol-phosphate transaminase {ECO:0000255|HAMAP-Rule:MF_01023};
GN Name=hisC {ECO:0000255|HAMAP-Rule:MF_01023};
GN OrderedLocusNames=Cgl2101, cg2304;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RA Han M.S., Jung S.I., Chun J.Y., Lee M.-S.;
RT "Molecular cloning of hisC gene from Corynebacterium glutamicum.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948641; DOI=10.1016/s0168-1656(03)00161-5;
RA McHardy A.C., Tauch A., Rueckert C., Puehler A., Kalinowski J.;
RT "Genome-based analysis of biosynthetic aminotransferase genes of
RT Corynebacterium glutamicum.";
RL J. Biotechnol. 104:229-240(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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:0000255|HAMAP-
CC Rule:MF_01023};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01023}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01023}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01023}.
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DR EMBL; AF160478; AAF80390.1; -; Genomic_DNA.
DR EMBL; AY238320; AAO92311.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99494.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20437.1; -; Genomic_DNA.
DR RefSeq; NP_601300.1; NC_003450.3.
DR RefSeq; WP_011014880.1; NC_006958.1.
DR PDB; 3CQ4; X-ray; 2.20 A; A/B=1-366.
DR PDB; 3CQ5; X-ray; 1.80 A; A/B/C=1-366.
DR PDB; 3CQ6; X-ray; 2.10 A; A/C/E=1-366.
DR PDBsum; 3CQ4; -.
DR PDBsum; 3CQ5; -.
DR PDBsum; 3CQ6; -.
DR AlphaFoldDB; Q9KJU4; -.
DR SMR; Q9KJU4; -.
DR STRING; 196627.cg2304; -.
DR KEGG; cgb:cg2304; -.
DR KEGG; cgl:Cgl2101; -.
DR PATRIC; fig|196627.13.peg.2038; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_1_11; -.
DR OMA; IWLNANE; -.
DR BRENDA; 2.6.1.9; 960.
DR UniPathway; UPA00031; UER00012.
DR EvolutionaryTrace; Q9KJU4; -.
DR Proteomes; UP000000582; Chromosome.
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 Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01141; hisC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aminotransferase;
KW Histidine biosynthesis; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..366
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_0000153350"
FT MOD_RES 228
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
FT CONFLICT 68..77
FT /note="AVELRDELAA -> VWNGDDAWLL (in Ref. 1; AAF80390)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="G -> E (in Ref. 1; AAF80390)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="R -> P (in Ref. 1; AAF80390)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..288
FT /note="ER -> DC (in Ref. 1; AAF80390)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:3CQ5"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:3CQ5"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:3CQ5"
FT HELIX 43..56
FT /evidence="ECO:0007829|PDB:3CQ5"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:3CQ5"
FT HELIX 69..83
FT /evidence="ECO:0007829|PDB:3CQ5"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:3CQ5"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:3CQ5"
FT HELIX 97..109
FT /evidence="ECO:0007829|PDB:3CQ5"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:3CQ5"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:3CQ5"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:3CQ5"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:3CQ5"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:3CQ5"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:3CQ5"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:3CQ5"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:3CQ5"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:3CQ5"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:3CQ5"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:3CQ5"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:3CQ5"
FT STRAND 220..228
FT /evidence="ECO:0007829|PDB:3CQ5"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:3CQ5"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:3CQ5"
FT HELIX 245..251
FT /evidence="ECO:0007829|PDB:3CQ5"
FT HELIX 261..272
FT /evidence="ECO:0007829|PDB:3CQ5"
FT HELIX 274..278
FT /evidence="ECO:0007829|PDB:3CQ5"
FT HELIX 280..298
FT /evidence="ECO:0007829|PDB:3CQ5"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:3CQ5"
FT STRAND 306..313
FT /evidence="ECO:0007829|PDB:3CQ5"
FT HELIX 318..327
FT /evidence="ECO:0007829|PDB:3CQ5"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:3CQ5"
FT HELIX 348..362
FT /evidence="ECO:0007829|PDB:3CQ5"
SQ SEQUENCE 366 AA; 39918 MW; 244555DF9A21BDFC CRC64;
MTKITLSDLP LREELRGEHA YGAPQLNVDI RLNTNENPYP PSEALVADLV ATVDKIATEL
NRYPERDAVE LRDELAAYIT KQTGVAVTRD NLWAANGSNE ILQQLLQAFG GPGRTALGFQ
PSYSMHPILA KGTHTEFIAV SRGADFRIDM DVALEEIRAK QPDIVFVTTP NNPTGDVTSL
DDVERIINVA PGIVIVDEAY AEFSPSPSAT TLLEKYPTKL VVSRTMSKAF DFAGGRLGYF
VANPAFIDAV MLVRLPYHLS ALSQAAAIVA LRHSADTLGT VEKLSVERVR VAARLEELGY
AVVPSESNFV FFGDFSDQHA AWQAFLDRGV LIRDVGIAGH LRTTIGVPEE NDAFLDAAAE
IIKLNL
