UniProt: E7CCN3

Database: UniProt
Entry: E7CCN3_SOLHA

LinkDB:  E7CCN3_SOLHA 
Original site:  E7CCN3_SOLHA

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (10)   
   InterPro (7)   
   Pfam (1)   
   PROSITE (2)   
Literature (1)   
   PubMed (1)   
All databases (18)   

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ID   E7CCN3_SOLHA            Unreviewed;       448 AA.
AC   E7CCN3;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   03-MAY-2023, entry version 47.
DE   RecName: Full=Arginine decarboxylase {ECO:0000256|ARBA:ARBA00012426, ECO:0000256|RuleBase:RU003740};
DE            EC=4.1.1.19 {ECO:0000256|ARBA:ARBA00012426, ECO:0000256|RuleBase:RU003740};
DE   Flags: Fragment;
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:ADV29057.1};
RN   [1] {ECO:0000313|EMBL:ADV29057.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=391b {ECO:0000313|EMBL:ADV29057.1}, 392a
RC   {ECO:0000313|EMBL:ADV29058.1}, and 392b {ECO:0000313|EMBL:ADV29059.1};
RA   Merino C.G., Staedler T., Tellier A., Stephan W.;
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADV29057.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=391b {ECO:0000313|EMBL:ADV29057.1}, 392a
RC   {ECO:0000313|EMBL:ADV29058.1}, and 392b {ECO:0000313|EMBL:ADV29059.1};
RX   PubMed=21245893; DOI=10.1038/hdy.2010.175;
RA   Tellier A., Fischer I., Merino C., Xia H., Camus-Kulandaivelu L.,
RA   Stadler T., Stephan W.;
RT   "Fitness effects of derived deleterious mutations in four closely related
RT   wild tomato species with spatial structure.";
RL   Heredity 107:189-199(2011).
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|ARBA:ARBA00001946,
CC         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|ARBA:ARBA00008357,
CC       ECO:0000256|RuleBase:RU003740}.
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DR   EMBL; GU950697; ADV29057.1; -; Genomic_DNA.
DR   EMBL; GU950698; ADV29058.1; -; Genomic_DNA.
DR   EMBL; GU950699; ADV29059.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7CCN3; -.
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   CDD; cd06830; PLPDE_III_ADC; 1.
DR   Gene3D; 1.20.58.930; -; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR002985; Arg_decrbxlase.
DR   InterPro; IPR022657; De-COase2_CS.
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.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793,
KW   ECO:0000256|RuleBase:RU003740};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003740};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU003740};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003740};
KW   Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066,
KW   ECO:0000256|RuleBase:RU003740}.
FT   DOMAIN          98..351
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ADV29057.1"
FT   NON_TER         448
FT                   /evidence="ECO:0000313|EMBL:ADV29057.1"
SQ   SEQUENCE   448 AA;  48783 MW;  4777A16AED52CB05 CRC64;
     WSPELSSDLY RIGGWGAPYF TVNSSGDISV RPHGTDTLPH QEIDLLKVVK KASDPINSGG
     LGLQLPLVVR FPDVLKNRLE SLQSAFDYAV QSEGYEAHYQ GVYPVKCNQD RFVVEDIVKF
     GSGFRFGLEA GSKPELLLAM SSLCKGSSEG LLVCNGFKDA EYISLALVAR KLQLNTVIVL
     EQEEELDLVI DISRKMAVQP VIGLRAKLRT KHSGHFGSTS GEKGKFGLTT TQILRVVRKL
     KESGMLDCLQ LLHFHIGSQI PSTELLADGV GEAAQVYSEL VRLGAGMKFI DIGGGLGIDY
     DGTKSSDSDV SVGYGLQDYA STVVQAVRFV CDRKNVKHPV ICSESGRAIV SHHSVLIFEA
     VSSTSTRSQE LSSMSLHSFV EKLNDDARAD YRNLSAAAIR GEYDTCMLYA DQLKQRCVEQ
     FKDGNLDIEQ LAAVDAVCDF VSKAIGAS
//

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