ID A7E9J3_SCLS1 Unreviewed; 426 AA.
AC A7E9J3;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
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=SS1G_01973 {ECO:0000313|EMBL:EDN97045.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN97045.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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 -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008392}.
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DR EMBL; CH476622; EDN97045.1; -; Genomic_DNA.
DR RefSeq; XP_001597777.1; XM_001597727.1.
DR AlphaFoldDB; A7E9J3; -.
DR STRING; 665079.A7E9J3; -.
DR EnsemblFungi; EDN97045; EDN97045; SS1G_01973.
DR GeneID; 5493590; -.
DR KEGG; ssl:SS1G_01973; -.
DR VEuPathDB; FungiDB:sscle_01g004630; -.
DR eggNOG; KOG0633; Eukaryota.
DR HOGENOM; CLU_017584_3_1_1; -.
DR InParanoid; A7E9J3; -.
DR OMA; NFVQFGR; -.
DR OrthoDB; 1203268at2759; -.
DR Proteomes; UP000001312; 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:EnsemblFungi.
DR GO; GO:0010045; P:response to nickel cation; IEA:EnsemblFungi.
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; IPR001917; Aminotrans_II_pyridoxalP_BS.
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.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 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:UP000001312};
KW Transferase {ECO:0000256|ARBA:ARBA00022576}.
FT DOMAIN 39..391
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 426 AA; 46542 MW; E02FBA9FCE201FE0 CRC64;
MPSRSDSPFN LQTCARPNIL SLEPYRCARD DYKDDGTNIL LDANENAYGP SLPGSTTSNP
SLNFLGLNRY PDPHQHPLKS LLCTLRNTHH HTELPLHPLN LFLGVGSDEA IDALLRCFCT
PSVDSILVCP PTYGMYSVSA QVNDVALVKV PLLPAPEFGL DVPAILDTLS KPQPKPIKLI
YICSPGNPTG SLIPKEQIEQ ILLHKTWNGI VVVDEAYIDF SPDGSSLAEW VNEWPNLVVL
QTLSKAFGLA GIRLGAAFAS VEVAALLNNL KAPYNISSPT EALASQALKE DGLSVMRTHK
EKIVGQRERL LKDLPKVKGV GRFRGGIASN FLLVEILNQS GKPDNEVARK VYETLAENRG
VVVRFRGKEH GCLGCLRITV GTEDEVTRFL GQVGGVIEQV WKGEGEKVES VEEEQKKEAE
ANNILA
//
