HIS8_METLZ
ID HIS8_METLZ Reviewed; 351 AA.
AC A2SSJ1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 83.
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=Mlab_1128;
OS Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX NCBI_TaxID=410358;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43576 / DSM 4855 / Z;
RX PubMed=21304657; DOI=10.4056/sigs.35575;
RA Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL Stand. Genomic Sci. 1:197-203(2009).
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 -!- 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; CP000559; ABN07297.1; -; Genomic_DNA.
DR RefSeq; WP_011833500.1; NC_008942.1.
DR AlphaFoldDB; A2SSJ1; -.
DR SMR; A2SSJ1; -.
DR STRING; 410358.Mlab_1128; -.
DR EnsemblBacteria; ABN07297; ABN07297; Mlab_1128.
DR GeneID; 4795647; -.
DR KEGG; mla:Mlab_1128; -.
DR eggNOG; arCOG04273; Archaea.
DR HOGENOM; CLU_017584_3_3_2; -.
DR OMA; IWLNANE; -.
DR OrthoDB; 69863at2157; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000000365; 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..351
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_1000149102"
FT MOD_RES 215
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ SEQUENCE 351 AA; 38283 MW; F38DB49D3F26DE53 CRC64;
MKPRVRSEFV KSGYVFAKSP ADIAKEYGFT EVAMLGSNEN PYPPSDKVLR AAEAELSGVN
RYPDPKAAAF HAALRTYICD CPVVTSGLGM DGVIETVIRT IVEPGDKVVI STPTFSMYGL
AAKAASARVV NVSRSADFSV DLDTFLNEAK DARLSFLCTP NNPTGTVTPV EDIEYILDRI
EGVLFLDCAY VEFSDINYLP LLSRDNLIIG RTMSKVYGLA GLRIGYAFVP EWLEAPYNIA
ATPFTMNRLS EAAASVAVSD AAYRESFIAH VQKWRDVFMQ EIPFPVYPSG SNFILINVAP
QKGDAAAESL AKHGVLVRSC TSFPGLGDTF IRVSVGADWE NERFLAAVKK L