HIS8_STRM5
ID HIS8_STRM5 Reviewed; 364 AA.
AC B4STN8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=Smal_1758;
OS Stenotrophomonas maltophilia (strain R551-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=391008;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R551-3;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001111; ACF51462.1; -; Genomic_DNA.
DR RefSeq; WP_012510884.1; NC_011071.1.
DR AlphaFoldDB; B4STN8; -.
DR SMR; B4STN8; -.
DR STRING; 391008.Smal_1758; -.
DR PRIDE; B4STN8; -.
DR EnsemblBacteria; ACF51462; ACF51462; Smal_1758.
DR KEGG; smt:Smal_1758; -.
DR eggNOG; COG0079; Bacteria.
DR HOGENOM; CLU_017584_3_1_6; -.
DR OMA; IWLNANE; -.
DR OrthoDB; 1248286at2; -.
DR BioCyc; SMAL391008:SMAL_RS09010-MON; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000001867; 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..364
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_1000135425"
FT MOD_RES 220
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ SEQUENCE 364 AA; 38208 MW; 95A9B9A63EB54411 CRC64;
MNADIDDVLA LVRPDLQAFA GYSSARSAAV QGEVWLNANE SAWANPADAA GNSRRYPEPQ
PLALREGLAA LYGVTPPQLL IGRGSDEAID LLVRALCVPG RDGVLVTPPV FGMYAVCARL
QGAALIEVPL VDTEDGLRAD LDAVIDTAKS RNAKLVFLCA PSNPAGSDIA LDEIERVATA
LRGQALVVVD EAYVEYAQRP SAATLLAAHA NLAVLRTLSK AHALAAARIG SLIAAPELIA
VLRRCQAPYP VPTPCAELAV QALQPAGLAR TAERVATVIA ERERLFAALP GLPGVRRVYR
SAGNYLLVRF ADAQAAFDTL LAAGVVVRDQ RAAPQLGDAL RISIGSPEEN DRVLAALSAR
RAAA