ID M1D441_SOLTU Unreviewed; 463 AA.
AC M1D441;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Histidine decarboxylase {ECO:0000313|EnsemblPlants:PGSC0003DMT400080887};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400080887, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400080887}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400080887};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR AlphaFoldDB; M1D441; -.
DR STRING; 4113.M1D441; -.
DR PaxDb; 4113-PGSC0003DMT400080887; -.
DR EnsemblPlants; PGSC0003DMT400080887; PGSC0003DMT400080887; PGSC0003DMG400031502.
DR Gramene; PGSC0003DMT400080887; PGSC0003DMT400080887; PGSC0003DMG400031502.
DR eggNOG; KOG0629; Eukaryota.
DR HOGENOM; CLU_591096_0_0_1; -.
DR InParanoid; M1D441; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
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 InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46101; -; 1.
DR PANTHER; PTHR46101:SF14; HISTIDINE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115}.
FT REGION 408..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 245
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 463 AA; 52301 MW; AAF80BFCE40CE59E CRC64;
MVVATKNGIN APSSPRENMC LSLIEPVKDK TSFEELNMIL TQYVETLSQR MKYHIGYPIN
LYYEHHAALG PLLQFHLNNF GDPFTQHPTD FHSKDFEVAV LDWFAQLWEI EKDEYWGYIT
SGGTEGNLHG LLVGRELLPD GIIYASTDSH YSIFKAARMY RMDLETINTL VNGEIDYEDL
RSKLLVNKNK PAIININFGT TYKGAIDDVD MILQILENCG YSNDRFYIHC DAALYGLIVP
FINHKVEYIA SIDNTISGSR NGLAPIFLWY SLSMKGHVGL QQDAKMFYEN ARYLKDRLHK
AGISAMLNEL SNIVVFERPC DDKFIRRWAT ILHKRYGTCC GYGFTIYKFS GAATTGFRPS
SNSPKTPIFS LPFLLQTRSK TPSGYSHFVI SGKIPVKSHL FSDQTTQQLP NTTISPPKND
QGSTTSPSLA KTSKYPPETN NSDSEQQLQR GNHVANNHKA PTS
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