HIS82_LEGPL
ID HIS82_LEGPL Reviewed; 369 AA.
AC Q5WV43;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Histidinol-phosphate aminotransferase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01023};
GN Name=hisC2 {ECO:0000255|HAMAP-Rule:MF_01023}; OrderedLocusNames=lpl1974;
OS Legionella pneumophila (strain Lens).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=297245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lens;
RX PubMed=15467720; DOI=10.1038/ng1447;
RA Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA Glaser P., Buchrieser C.;
RT "Evidence in the Legionella pneumophila genome for exploitation of host
RT cell functions and high genome plasticity.";
RL Nat. Genet. 36:1165-1173(2004).
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; CR628337; CAH16214.1; -; Genomic_DNA.
DR RefSeq; WP_011215962.1; NC_006369.1.
DR AlphaFoldDB; Q5WV43; -.
DR SMR; Q5WV43; -.
DR EnsemblBacteria; CAH16214; CAH16214; lpl1974.
DR KEGG; lpf:lpl1974; -.
DR LegioList; lpl1974; -.
DR HOGENOM; CLU_017584_3_3_6; -.
DR OMA; NYHVAGF; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000002517; 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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Histidine biosynthesis;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..369
FT /note="Histidinol-phosphate aminotransferase 2"
FT /id="PRO_0000153378"
FT MOD_RES 231
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ SEQUENCE 369 AA; 41435 MW; 7D7826AEFB8430CD CRC64;
MSIDFQQLPH AGIRSLIPYV PGKSIEELAK EKGITDIIKL ASNENPLGCS PLALSAIQTM
SSHYIATYPS PWNHPLMSKL ASYLKVKPEQ LFLSNGSDYL FNILLNCFAL HTDRHILTHD
YAFSTYAIQA NSLQIPINSV PIGHNWEVNI TDIVNACNQK TGIIFIANPN NPTGVLIQQE
EIKYLLEQIP KSTLLVLDEA YYEFAASQLT VNSLDWLEEH PNLVVTRTFS KIYGMAGLRL
GYAIANPSII NILKRVQLPF IVNQVALAAA YAAIDDDDFI QSSLKMNNEG MSQLQAGFNE
LNIKYLPSSC NFLTFDCEED SMALYNYLLD NGIIVRPLHA YKMNNFIRVT IGTKEQNSRF
LTALKNFYL
