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Database: UniProt
Entry: B9VD26_SOLHA
LinkDB: B9VD26_SOLHA
Original site: B9VD26_SOLHA 
ID   B9VD26_SOLHA            Unreviewed;       222 AA.
AC   B9VD26;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Arginine decarboxylase {ECO:0000256|RuleBase:RU003740};
DE            EC=4.1.1.19 {ECO:0000256|RuleBase:RU003740};
DE   Flags: Fragment;
GN   Name=adc1 {ECO:0000313|EMBL:ACM16871.1};
OS   Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=62890 {ECO:0000313|EMBL:ACM16871.1};
RN   [1] {ECO:0000313|EMBL:ACM16871.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Zuriaga E., Blanca J.M., Nuez F.;
RT   "Classification and phylogenetic relationships in Solanum section
RT   Lycopersicon based on AFLP and two nuclear gene sequences.";
RL   Genet. Resour. Crop Evol. 0:0-0(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-arginine = agmatine + CO2; Xref=Rhea:RHEA:17641,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:58145; EC=4.1.1.19;
CC         Evidence={ECO:0000256|ARBA:ARBA00000009,
CC         ECO:0000256|RuleBase:RU003740};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU003740};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU003740};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC       agmatine from L-arginine: step 1/1. {ECO:0000256|ARBA:ARBA00004773,
CC       ECO:0000256|RuleBase:RU003740}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       SpeA subfamily. {ECO:0000256|RuleBase:RU003740}.
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DR   EMBL; FJ533300; ACM16871.1; -; Genomic_DNA.
DR   EMBL; FJ533301; ACM16872.1; -; Genomic_DNA.
DR   EMBL; FJ533302; ACM16873.1; -; Genomic_DNA.
DR   EMBL; FJ533303; ACM16874.1; -; Genomic_DNA.
DR   EMBL; FJ533304; ACM16875.1; -; Genomic_DNA.
DR   EMBL; FJ533305; ACM16876.1; -; Genomic_DNA.
DR   EMBL; FJ533306; ACM16877.1; -; Genomic_DNA.
DR   EMBL; FJ533307; ACM16878.1; -; Genomic_DNA.
DR   EMBL; FJ533308; ACM16879.1; -; Genomic_DNA.
DR   EMBL; FJ533309; ACM16880.1; -; Genomic_DNA.
DR   EMBL; FJ533310; ACM16881.1; -; Genomic_DNA.
DR   EMBL; FJ533311; ACM16882.1; -; Genomic_DNA.
DR   EMBL; FJ533316; ACM16887.1; -; Genomic_DNA.
DR   EMBL; FJ533317; ACM16888.1; -; Genomic_DNA.
DR   EMBL; FJ533342; ACM16913.1; -; Genomic_DNA.
DR   EMBL; FJ533343; ACM16914.1; -; Genomic_DNA.
DR   EMBL; FJ533384; ACM16955.1; -; Genomic_DNA.
DR   EMBL; FJ533385; ACM16956.1; -; Genomic_DNA.
DR   EMBL; FJ533436; ACM17007.1; -; Genomic_DNA.
DR   EMBL; FJ533437; ACM17008.1; -; Genomic_DNA.
DR   EMBL; FJ533444; ACM17015.1; -; Genomic_DNA.
DR   EMBL; FJ533445; ACM17016.1; -; Genomic_DNA.
DR   EMBL; FJ533452; ACM17023.1; -; Genomic_DNA.
DR   EMBL; FJ533453; ACM17024.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9VD26; -.
DR   UniPathway; UPA00186; UER00284.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR002985; Arg_decrbxlase.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR   InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   PANTHER; PTHR43295; ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43295:SF1; ARGININE DECARBOXYLASE 1-RELATED; 1.
DR   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   PRINTS; PR01180; ARGDCRBXLASE.
DR   PRINTS; PR01179; ODADCRBXLASE.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS00878; ODR_DC_2_1; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|RuleBase:RU003740};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003740};
KW   Magnesium {ECO:0000256|RuleBase:RU003740};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003740};
KW   Spermidine biosynthesis {ECO:0000256|RuleBase:RU003740}.
FT   DOMAIN          77..219
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACM16871.1"
FT   NON_TER         222
FT                   /evidence="ECO:0000313|EMBL:ACM16871.1"
SQ   SEQUENCE   222 AA;  24326 MW;  CB53705324C28AC2 CRC64;
     VNSSGDISVR PHGTDTLPHQ EIDLLKVVKK ASDPINSGGL GLQLPLVVRF PDVLKNRLES
     LQSAFDYAVQ SEGYEAHYQG VYPVKCNQDR FVVEDIVKFG SGFRFGLEAG SKPELLLAMS
     SLCKGSSEGL LVCNGFKDAE YISLALVARK LQLNTVIVLE QEEELDLVID ISRKMAVQPV
     IGLRAKLRTK HSGHFGSTSG EKGKFGLTTT QILRVVRKLK ES
//
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