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Database: UniProt
Entry: A0A090M7D0_OSTTA
LinkDB: A0A090M7D0_OSTTA
Original site: A0A090M7D0_OSTTA 
ID   A0A090M7D0_OSTTA        Unreviewed;       414 AA.
AC   A0A090M7D0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=histidinol-phosphate transaminase {ECO:0000256|ARBA:ARBA00012748};
DE            EC=2.6.1.9 {ECO:0000256|ARBA:ARBA00012748};
DE   AltName: Full=Imidazole acetol-phosphate transaminase {ECO:0000256|ARBA:ARBA00030262};
GN   ORFNames=OT_ostta02g01690 {ECO:0000313|EMBL:CEG00992.1};
OS   Ostreococcus tauri.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Ostreococcus.
OX   NCBI_TaxID=70448 {ECO:0000313|EMBL:CEG00992.1, ECO:0000313|Proteomes:UP000009170};
RN   [1] {ECO:0000313|Proteomes:UP000009170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OTTH0595 {ECO:0000313|Proteomes:UP000009170};
RX   PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA   Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA   Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA   Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA   Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA   Van de Peer Y., Moreau H.;
RT   "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT   unveils many unique features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001045};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
CC       {ECO:0000256|ARBA:ARBA00005011}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CEG00992.1}.
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DR   EMBL; CAID01000002; CEG00992.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090M7D0; -.
DR   STRING; 70448.A0A090M7D0; -.
DR   InParanoid; A0A090M7D0; -.
DR   OrthoDB; 1203268at2759; -.
DR   Proteomes; UP000009170; Chromosome 2.
DR   GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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   NCBIfam; TIGR01141; hisC; 1.
DR   PANTHER; PTHR42885:SF2; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42885; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009170};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CEG00992.1}.
FT   DOMAIN          82..405
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   414 AA;  46273 MW;  1AA4E59F08BE6EC0 CRC64;
     MSARFRLAHN PKMYLNGRGV PHRQKSSTSR TNSSHSRAKS SRTSNELITT DFVRKHIINL
     QPYTPIIPFE VLSEQLQRPT SEIIKLDANE NPYGPPPEVY DALRTVTYPH IYPDPESRRL
     RAMLSSECKV PAENLLVGCG ADELIDLLLR VVLEPGDKVI NTPPTFGMYS FDSYINDGCV
     IDVKRGPAPS FRVDVDGIER AVAEHNPKIL FLTSPNNPDG SVLDESDLER LLCLPVLVVL
     DEAYVEFSSS YTSRIAEVPN RKNLIVLRTF SKRAGLAGIR VGYGAFPNEL IEFIWRVKQP
     YNVSVIAEEA AMAALSNPTY LQDVRDKIVC ERARLFTLLS QFDFMDPFPS ESNFILCRVT
     GASAEFIKKS LLARGIVIRY YSSPKEISDC IRISVGRPED TDAIIAGLTS ISSK
//
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