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HIS81_MANSM
ID   HIS81_MANSM             Reviewed;         366 AA.
AC   Q65S79;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Histidinol-phosphate aminotransferase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01023};
GN   Name=hisC1 {ECO:0000255|HAMAP-Rule:MF_01023}; OrderedLocusNames=MS1574;
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E;
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(2004).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAU38181.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE016827; AAU38181.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041640217.1; NC_006300.1.
DR   AlphaFoldDB; Q65S79; -.
DR   SMR; Q65S79; -.
DR   STRING; 221988.MS1574; -.
DR   EnsemblBacteria; AAU38181; AAU38181; MS1574.
DR   KEGG; msu:MS1574; -.
DR   eggNOG; COG0079; Bacteria.
DR   HOGENOM; CLU_017584_3_3_6; -.
DR   OrthoDB; 1248286at2; -.
DR   UniPathway; UPA00031; UER00012.
DR   Proteomes; UP000000607; 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:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
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; IPR004838; NHTrfase_class1_PyrdxlP-BS.
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..366
FT                   /note="Histidinol-phosphate aminotransferase 1"
FT                   /id="PRO_0000153388"
FT   MOD_RES         226
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ   SEQUENCE   366 AA;  40606 MW;  62E34E766C0B45C5 CRC64;
     MTFLQQANTG VQALSPYQAG KPIEELEREL GISNIIKLAS NENPFGFPES AKKAIQNQLD
     NLTRYPDSNG FSLKAAIAEK FNLQPEQITL GNGSNDLIEL IAHTFATEGD EIIFSQYAFI
     VYPLITKAIN AKAREIPAKN WGHDLEAFLA AINEKTKLIF IANPNNPTGN FLTEAEIDSF
     LAKVPPHIVV ALDEAYTEFT AKEERVNSLA LLKKYPNLVV SRSLSKAYGL AGLRIGFAVS
     NPEIAGLFNR VRQPFNVNSL ALAAAEAVLN DDDFVEKAAE NNRRELKRYE EFCQKYGLQY
     IPSKGNFITI DFQQPAAPVY DALLHEGVIV RPIAGYGMPN HLRISIGLPE ENQRLFDALI
     KILNLK
 
 
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