ID A0A1S4BUX2_TOBAC Unreviewed; 456 AA.
AC A0A1S4BUX2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Histidine decarboxylase-like {ECO:0000313|RefSeq:XP_016492676.1};
GN Name=LOC107812155 {ECO:0000313|RefSeq:XP_016492676.1};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097 {ECO:0000313|Proteomes:UP000084051, ECO:0000313|RefSeq:XP_016492676.1};
RN [1] {ECO:0000313|Proteomes:UP000084051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TN90 {ECO:0000313|Proteomes:UP000084051};
RX PubMed=24807620; DOI=10.1038/ncomms4833;
RA Sierro N., Battey J.N., Ouadi S., Bakaher N., Bovet L., Willig A.,
RA Goepfert S., Peitsch M.C., Ivanov N.V.;
RT "The tobacco genome sequence and its comparison with those of tomato and
RT potato.";
RL Nat. Commun. 5:3833-3833(2014).
RN [2] {ECO:0000313|RefSeq:XP_016492676.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, 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 RefSeq; XP_016492676.1; XM_016637190.1.
DR AlphaFoldDB; A0A1S4BUX2; -.
DR SMR; A0A1S4BUX2; -.
DR STRING; 4097.A0A1S4BUX2; -.
DR PaxDb; 4097-A0A1S4BUX2; -.
DR GeneID; 107812155; -.
DR KEGG; nta:107812155; -.
DR OMA; FWRKYTQ; -.
DR OrthoDB; 750143at2759; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0016831; F:carboxy-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 InterPro; IPR021115; Pyridoxal-P_BS.
DR PANTHER; PTHR46101; -; 1.
DR PANTHER; PTHR46101:SF16; HISTIDINE DECARBOXYLASE-LIKE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 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:UP000084051}.
FT REGION 16..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 281
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 456 AA; 51423 MW; 64EA2E5E1199E578 CRC64;
MGSLSFEKDF EVSAITPPSL FPNGDNKRQK LEPPGPRKNL QLAVTEPGFG SDGPSLDSIL
VNYLDTLTQR VNFHIGYPVN ICYHHYATLA PLLQFHLNNC GDPFIDNTVD FHSKDFEMAV
LDWFANLWEI EKDQYWGYVT NGGTEGNLHG ILLGRELLPD GILYASKDSH YSVFKAARMY
RMDSETINTS VNGEMDYSDL RTKLLQNKDK PAIINVTIGT TFKGAVDDLD IILQTLKDCG
YSQDMFYIHC DAALCGLIVP FINNMISFKK SIGSVTISGH KFLGCPMPCG VQITRKSYIN
NLSRNVEYIA SVDATISGSR NGLTPIFLWY SLSAKGQIGL QKDVKRCLDN AIYLKDRLQQ
AGISVMLNEL SIIVVLERPR DHEFVRRWQL SCMKDMAHVI VMPDITRETL DNFVNDLVQQ
RKLWYQHGRV TTPCIADDIG AQNCSCSYHK IDYIIS
//
