HIS8_STAA8
ID HIS8_STAA8 Reviewed; 352 AA.
AC Q2G087;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=SAOUHSC_00733;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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; CP000253; ABD29866.1; -; Genomic_DNA.
DR RefSeq; WP_000663030.1; NZ_LS483365.1.
DR RefSeq; YP_499293.1; NC_007795.1.
DR AlphaFoldDB; Q2G087; -.
DR SMR; Q2G087; -.
DR STRING; 1280.SAXN108_0792; -.
DR EnsemblBacteria; ABD29866; ABD29866; SAOUHSC_00733.
DR GeneID; 3920978; -.
DR KEGG; sao:SAOUHSC_00733; -.
DR PATRIC; fig|93061.5.peg.662; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_3_9; -.
DR OMA; YPDMACT; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000008816; 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; 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 Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01141; hisC; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..352
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_1000063505"
FT MOD_RES 221
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ SEQUENCE 352 AA; 39788 MW; D6AA6041524D4700 CRC64;
MKEQLNQLSA YQPGLSPRAL KEKYGIEGDL YKLASNENLY GPSPKVKEAI SAHLDELYYY
PETGSPTLKA AISKHLNVDQ SRILFGAGLD EVILMISRAV LTPGDTIVTS EATFGQYYHN
AIVESANVIQ VPLKDGGFDL EGILKEVNED TSLVWLCNPN NPTGTYFNHE SLDSFLSQVP
PHVPVIIDEA YFEFVTAEDY PDTLALQQKY DNAFLLRTFS KAYGLAGLRV GYVVASEHAI
EKWNIIRPPF NVTRISEYAA VAALEDQQYL KEVTHKNSVE RERFYQLPQS EYFLPSQTNF
IFVKTKRVNE LYEALLNVGC ITRPFPTGVR ITIGFKEQND KMLEVLSNFK YE