ID A0A1S3XUG6_TOBAC Unreviewed; 465 AA.
AC A0A1S3XUG6;
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_016443588.1};
GN Name=LOC107768931 {ECO:0000313|RefSeq:XP_016443588.1};
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_016443588.1};
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_016443588.1}
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_016443588.1; XM_016588102.1.
DR AlphaFoldDB; A0A1S3XUG6; -.
DR SMR; A0A1S3XUG6; -.
DR STRING; 4097.A0A1S3XUG6; -.
DR PaxDb; 4097-A0A1S3XUG6; -.
DR GeneID; 107768931; -.
DR KEGG; nta:107768931; -.
DR OMA; AKMYRMK; -.
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:SF5; 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 MOD_RES 290
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 465 AA; 52168 MW; BDB4018099EAFC53 CRC64;
MGSLSFEKEF EPSAVTPRGL APPGLIGNGD FGEMKRLKVA TPTAPRKNLN ITVTEPGSRN
DGQSLDCILM NYIDTLSQRI NYHIGYPVNI CYEHYASLAP LLQFHLNNCG DPFLQNTVDF
HSKDFEVAVL NWFADLWEIE KDQYWGYVTN GGTEGNLHGI LVGRELLPTG ILYASKDSHY
SVAKAAMMYR MDFEMVNTSV HGEMDYSDLK VKLLQNKGKP AIINVTIGTT FKGAVDDLDV
ILQTLKDCGY TYDQFYIHCD AALNGLIIPF IKNMISFKKP IGSVTISGHK FLGCPMPCGI
QITRKSYINN LSRKVEYIAS VDATISGSRN GLAPIFLWYS LSAKGQVGLQ KDVKRCLDNA
KYLKDRLQQA GISVMLNELS IIVVLERPRD HEFVRRWQLS CVRDMAHVIV MPGITREILD
SFINDLLQQR KKWYKDGNVT PPCVAEDIGA QNCACSYHKI DFIIP
//