HIS81_RALSO
ID HIS81_RALSO Reviewed; 374 AA.
AC Q8XV80;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Histidinol-phosphate aminotransferase 1;
DE EC=2.6.1.9;
DE AltName: Full=Imidazole acetol-phosphate transaminase 1;
GN Name=hisC1; OrderedLocusNames=RSc2951; ORFNames=RS00135;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
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;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. Histidinol-phosphate aminotransferase
CC subfamily. {ECO:0000305}.
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DR EMBL; AL646052; CAD16658.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8XV80; -.
DR SMR; Q8XV80; -.
DR STRING; 267608.RSc2951; -.
DR EnsemblBacteria; CAD16658; CAD16658; RSc2951.
DR KEGG; rso:RSc2951; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_1_4; -.
DR OMA; IWLNANE; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000001436; 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; Reference proteome; Transferase.
FT CHAIN 1..374
FT /note="Histidinol-phosphate aminotransferase 1"
FT /id="PRO_0000153430"
FT MOD_RES 232
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 374 AA; 40441 MW; 0B39486908D44E93 CRC64;
MNANAPVQPS LDDLLGRIVR DDVRAMGAYH VPDASGMVKL DAMENPYHLP AMLRDALGKR
LAEVALNRYP VPTADALKAQ LKRVMRVPAG ADVLLGNGSD EIISLIAIAA AKPGATVLAP
VPGFVMYAMS AQLMGLKFVG VPLRADLTLD REAMLAAMAE HQPAVIYLAY PNNPTGNLFD
AADMDALLRA ARGPVCQSLV VVDEAYQPFA QHSWMPRLPE FDHLLVMRTV SKLGLAGIRL
GYVAGHPKWI AELDKVRPPY NVNVLTEATA AFVLDHVDVL DAQAATLRAE RTRLIDALSA
QPGVTVFPSA ANFLLLRVPD AAGLFERLLK RRVLVKNVSK MHPLLANCLR VTVSNPEENA
QFLDAFAASL QDTP
