HIS8_MAGSA
ID HIS8_MAGSA Reviewed; 363 AA.
AC Q2W047;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=amb3974;
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=342108;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
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; AP007255; BAE52778.1; -; Genomic_DNA.
DR RefSeq; WP_011386328.1; NC_007626.1.
DR AlphaFoldDB; Q2W047; -.
DR SMR; Q2W047; -.
DR STRING; 342108.amb3974; -.
DR EnsemblBacteria; BAE52778; BAE52778; amb3974.
DR KEGG; mag:amb3974; -.
DR HOGENOM; CLU_017584_3_3_5; -.
DR OMA; YPDMACT; -.
DR OrthoDB; 1248286at2; -.
DR UniPathway; UPA00031; UER00012.
DR Proteomes; UP000007058; 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..363
FT /note="Histidinol-phosphate aminotransferase"
FT /id="PRO_0000319771"
FT MOD_RES 220
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01023"
SQ SEQUENCE 363 AA; 38250 MW; 0E673E16AB26FE12 CRC64;
MTAPAPRPGI MDIRPYVGGE SAIEGVDRIL KLSSNEGALG PSPKAMEALR AMAPEMHRYP
DGGAEDLRKA IGARFGLDAS RIVCGAGSDE LLGILCRAYA GPGDEVLYSA HGFLMYAIAA
KACGATPVTA PEVDLTANVD NLLAAVTPRT KILFLANPNN PTGTYLPATE VARLRAGLRA
DILLVIDAAY TEFVSRNDYS GGIELVEAGD NVVVCRTFSK MYALGGLRLG WAYCPENVAG
VLNRVRNPFN VGAPALAAGL AAFNDTAYAE LCKSHNDYWL PWLSGQLAEL GLTVVPSVCN
FILVRFPKDA GKDAGAADKF LRSKGIIVRA MGGYGLGDCL RITIGTGEEN QLVVAALKEF
VGA