HIS8_LISIN
ID HIS8_LISIN Reviewed; 360 AA.
AC Q92A83;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 114.
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}; OrderedLocusNames=lin2039;
OS Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-680 / CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; AL596170; CAC97269.1; -; Genomic_DNA.
DR PIR; AE1687; AE1687.
DR RefSeq; WP_010991721.1; NC_003212.1.
DR PDB; 3FFH; X-ray; 2.31 A; A/B=1-360.
DR PDBsum; 3FFH; -.
DR AlphaFoldDB; Q92A83; -.
DR SMR; Q92A83; -.
DR STRING; 272626.lin2039; -.
DR EnsemblBacteria; CAC97269; CAC97269; CAC97269.
DR KEGG; lin:hisC; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_3_9; -.
DR OMA; IWLNANE; -.
DR OrthoDB; 1248286at2; -.
DR UniPathway; UPA00031; UER00012.
DR EvolutionaryTrace; Q92A83; -.
DR Proteomes; UP000002513; 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; Transferase.
FT CHAIN 1..360
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_0000153385"
FT MOD_RES 222
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:3FFH"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:3FFH"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:3FFH"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:3FFH"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:3FFH"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3FFH"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:3FFH"
FT HELIX 90..101
FT /evidence="ECO:0007829|PDB:3FFH"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:3FFH"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:3FFH"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:3FFH"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:3FFH"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:3FFH"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:3FFH"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:3FFH"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:3FFH"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3FFH"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:3FFH"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:3FFH"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:3FFH"
FT HELIX 238..246
FT /evidence="ECO:0007829|PDB:3FFH"
FT HELIX 255..266
FT /evidence="ECO:0007829|PDB:3FFH"
FT HELIX 268..291
FT /evidence="ECO:0007829|PDB:3FFH"
FT STRAND 302..308
FT /evidence="ECO:0007829|PDB:3FFH"
FT HELIX 313..322
FT /evidence="ECO:0007829|PDB:3FFH"
FT TURN 330..334
FT /evidence="ECO:0007829|PDB:3FFH"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:3FFH"
FT HELIX 346..359
FT /evidence="ECO:0007829|PDB:3FFH"
SQ SEQUENCE 360 AA; 40063 MW; 5CB77E883D507F2D CRC64;
MKWKKSLAGL SSYKPGKREE EVMAELGLTK ITKLSSNENP LGTSKKVAAI QANSSVETEI
YPDGWASSLR KEVADFYQLE EEELIFTAGV DELIELLTRV LLDTTTNTVM ATPTFVQYRQ
NALIEGAEVR EIPLLQDGEH DLEGMLNAID EKTTIVWICN PNNPTGNYIE LADIQAFLDR
VPSDVLVVLD EAYIEYVTPQ PEKHEKLVRT YKNLIITRTF SKIYGLASAR VGYGIADKEI
IRQLNIVRPP FNTTSIGQKL AIEAIKDQAF IGECRTSNAN GIKQYEAFAK RFEKVKLYPA
NGNFVLIDLG IEAGTIFSYL EKNGYITRSG AALGFPTAVR ITIGKEEDNS AVIALLEKLL
