ID R0GH67_9BRAS Unreviewed; 413 AA.
AC R0GH67;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=CARUB_v10020377mg {ECO:0000313|EMBL:EOA35222.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA35222.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
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; KB870806; EOA35222.1; -; Genomic_DNA.
DR RefSeq; XP_006302324.1; XM_006302262.1.
DR AlphaFoldDB; R0GH67; -.
DR STRING; 81985.R0GH67; -.
DR GeneID; 17896392; -.
DR KEGG; crb:17896392; -.
DR eggNOG; KOG0633; Eukaryota.
DR OrthoDB; 1203268at2759; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
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:UP000029121};
KW Transferase {ECO:0000256|ARBA:ARBA00022576}.
FT DOMAIN 86..407
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 413 AA; 46093 MW; 4F7991A31143E49F CRC64;
MGVINVQGAP SFSIHSSESN LRKSRALRKS ISRVYCLQSS SAAVDEPKNI TMGDSFIRPH
LRQLAAYQPI LPFEVLSAQL GRKPEDIVKL DANENPYGPP PEVFEALGNM KFPYVYPDPQ
SRRLRGALAQ DSGLEPEYIL VGCGADELID LIMRCVLDPG EKIIDCPPTF SMYVFDAAVN
AAGVIKVPRN PDFSLNVDRI AEVVELEKPK CIFLTSPNNP DGSVISEDDL LKILKMPILV
VLDEAYIEFS GIESRMKWVK KYENLIVLRT FSKRAGLAGL RVGYGAFPLS IIEYLWRAKQ
PYNVSVAGEV AALAALSNGK YLEDVRDALV RERERLFGLL KEVPFLNPYP SHSNFILCEV
TSGMDAKKLK EDLAKMGVMV RHYNSKELKG YVRVSAGKPE HTDVLMDCLK QFY
//
