HIS8_BAUCH
ID HIS8_BAUCH Reviewed; 360 AA.
AC Q1LT68;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-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}; OrderedLocusNames=BCI_0403;
OS Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX NCBI_TaxID=374463;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H.,
RA Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.;
RT "Metabolic complementarity and genomics of the dual bacterial symbiosis of
RT sharpshooters.";
RL PLoS Biol. 4:1079-1092(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; CP000238; ABF14107.1; -; Genomic_DNA.
DR RefSeq; WP_011520579.1; NC_007984.1.
DR AlphaFoldDB; Q1LT68; -.
DR SMR; Q1LT68; -.
DR STRING; 374463.BCI_0403; -.
DR EnsemblBacteria; ABF14107; ABF14107; BCI_0403.
DR KEGG; bci:BCI_0403; -.
DR HOGENOM; CLU_017584_3_1_6; -.
DR OMA; IWLNANE; -.
DR OrthoDB; 1248286at2; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000002427; 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..360
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_1000063463"
FT MOD_RES 213
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ SEQUENCE 360 AA; 40496 MW; 7CF6EB03501FD99E CRC64;
MSILNLARTN VLTLEPYQSA RRIGGGSQGN IWLNANEYPQ PTFYMLRSSN LNRYPDCQPQ
ELLNSYAAYA GVQPNQVLAC RGADEGIELL IRTFCEPSKD KILFCPPTYG MYRVSAETFG
VAYCAIQALD NWQLDLDTIY AQLDCVKLIY ICHPNNPTGN IINPSDIRQL LDITHGRTIL
VVDEAYIDFY PTASISSWIN HYPHLVILRT LSKAFALAGL RCGFILANPD IIKLLLKVIA
PYPISRPVVD IAKQALSTKG IHQTKRRVAN IDINRNWLIQ QLAECSCVSV VFPSVTNYLL
VRFHPNYHVF QSLWKKGTIL RDQNQQIGLA NCLRITIGTS LECQNLLTAL QALTLVSHKE