HIS8_METPE
ID HIS8_METPE Reviewed; 351 AA.
AC B8GIB0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=Mpal_0067;
OS Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX NCBI_TaxID=521011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c;
RX PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA Yavitt J.B., Zinder S.H.;
RT "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL Genome Announc. 3:0-0(2015).
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; CP001338; ACL15461.1; -; Genomic_DNA.
DR RefSeq; WP_012616780.1; NC_011832.1.
DR AlphaFoldDB; B8GIB0; -.
DR SMR; B8GIB0; -.
DR STRING; 521011.Mpal_0067; -.
DR EnsemblBacteria; ACL15461; ACL15461; Mpal_0067.
DR GeneID; 7272236; -.
DR KEGG; mpl:Mpal_0067; -.
DR eggNOG; arCOG04273; Archaea.
DR HOGENOM; CLU_017584_3_3_2; -.
DR OMA; IWLNANE; -.
DR OrthoDB; 69863at2157; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000002457; 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.
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_1000149104"
FT MOD_RES 214
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ SEQUENCE 351 AA; 38240 MW; 37FAE53C9F872B34 CRC64;
MQPSIRSYLR TGPGYVYAAH SGTARETGRI ACLASNENPF PPSEAAIAAG AAALATVNRY
PDDRMTDLTE ALKRLHGDHT FVVGNGMDGI IETVLRCFIG HGDRVVVSTP TFSFYGIAAA
GQGAIVENIQ RKEDFTVDIP AFTRACTGAK VAFLCTPNNP TGTVTTPAEV RKVLDGIGDC
MLFLDNAYVD FARDDYRPLM GEYENLIIGR TMSKIFGLAG LRVGYAFIPA WLEPFYMKAA
TPFSGISSVS AAAAVAALAD REHRERTLAH MLEWRERVRS AVRFPVLPSE ANFLMIDVAP
HTADDVVATL AGRGVLIRSC RSFPGLGDHY VRVSIGDAWE NERFIEEINR I