ID A0A058ZX88_EUCGR Unreviewed; 416 AA.
AC A0A058ZX88;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=EUGRSUZ_L00028 {ECO:0000313|EMBL:KCW46054.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW46054.1};
RN [1] {ECO:0000313|EMBL:KCW46054.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW46054.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KK198764; KCW46054.1; -; Genomic_DNA.
DR RefSeq; XP_010039333.1; XM_010041031.2.
DR AlphaFoldDB; A0A058ZX88; -.
DR STRING; 71139.A0A058ZX88; -.
DR EnsemblPlants; KCW46054; KCW46054; EUGRSUZ_L00028.
DR Gramene; KCW46054; KCW46054; EUGRSUZ_L00028.
DR eggNOG; KOG0633; Eukaryota.
DR InParanoid; A0A058ZX88; -.
DR OMA; FAIAHEP; -.
DR OrthoDB; 1203268at2759; -.
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 Transferase {ECO:0000256|ARBA:ARBA00022576}.
FT DOMAIN 88..407
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 416 AA; 46155 MW; 2ECB5641741B401E CRC64;
MGVVEISSFS ALWSAKLSGA RQPVCSLEGR RRGVVAMAST VDVQHLSEAN RELTGDSFIR
PHLRKLSPYQ PILPFEVLST RLGRKPEDII KLDANENPYG PPPEVFEALG SMKFPYVYPD
PESRRLRAAL AVDSGLEADY ILAGCGADEL IDLIMRCVLD PGDKIVDCPP TFTMYEFDAA
VNGAHVVKVP RKPDFSLNVE LIADAVEKEN PKCIFLTSPN NPDGSIIGDE DLIKILKLPV
LVVLDEAYIE FSGIESRMKW VKKYENLIVL RTFSKRAALA GLRVGYGAFP LSIIEYLWRA
KQPYNVSVAA EVAACAALQN PTYLEDVKDA LVQERERLFK LLKGVPFLNP YPSHSNFILC
EVTSGMDAKK LKEDLAKMGV MIRHYNNKEL KGYVRVSVGK PEHTAALMDG LSRLSL
//
