ID   SPEA_VIBVU              Reviewed;         640 AA.
AC   Q8DA54;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Biosynthetic arginine decarboxylase {ECO:0000255|HAMAP-Rule:MF_01417};
DE            Short=ADC {ECO:0000255|HAMAP-Rule:MF_01417};
DE            EC=4.1.1.19 {ECO:0000255|HAMAP-Rule:MF_01417};
GN   Name=speA {ECO:0000255|HAMAP-Rule:MF_01417}; OrderedLocusNames=VV1_2356;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SEQUENCE REVISION.
RC   STRAIN=CMCP6;
RX   PubMed=21245845; DOI=10.1038/msb.2010.115;
RA   Kim H.U., Kim S.Y., Jeong H., Kim T.Y., Kim J.J., Choy H.E., Yi K.Y.,
RA   Rhee J.H., Lee S.Y.;
RT   "Integrative genome-scale metabolic analysis of Vibrio vulnificus for drug
RT   targeting and discovery.";
RL   Mol. Syst. Biol. 7:460-460(2011).
CC   -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine.
CC       {ECO:0000255|HAMAP-Rule:MF_01417}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01417};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01417};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01417};
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       SpeA subfamily. {ECO:0000255|HAMAP-Rule:MF_01417}.
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DR   EMBL; AE016795; AAO10730.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q8DA54; -.
DR   SMR; Q8DA54; -.
DR   EnsemblBacteria; AAO10730; AAO10730; VV1_2356.
DR   KEGG; vvu:VV1_2356; -.
DR   HOGENOM; CLU_027243_1_0_6; -.
DR   SABIO-RK; Q8DA54; -.
DR   Proteomes; UP000002275; Chromosome 1.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06830; PLPDE_III_ADC; 1.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_01417; SpeA; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR040634; Arg_decarb_HB.
DR   InterPro; IPR041128; Arg_decarbox_C.
DR   InterPro; IPR002985; Arg_decrbxlase.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   PANTHER; PTHR43295; PTHR43295; 1.
DR   Pfam; PF17810; Arg_decarb_HB; 1.
DR   Pfam; PF17944; Arg_decarbox_C; 1.
DR   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   PIRSF; PIRSF001336; Arg_decrbxlase; 1.
DR   PRINTS; PR01180; ARGDCRBXLASE.
DR   PRINTS; PR01179; ODADCRBXLASE.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR01273; speA; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Magnesium; Metal-binding; Polyamine biosynthesis;
KW   Pyridoxal phosphate; Spermidine biosynthesis.
FT   CHAIN           1..640
FT                   /note="Biosynthetic arginine decarboxylase"
FT                   /id="PRO_0000149985"
FT   BINDING         290..300
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT   MOD_RES         105
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ   SEQUENCE   640 AA;  72493 MW;  3157EA5825FFF912 CRC64;
     MRLDVEQTSK LDRVRADYNV HYWSQGFYGI DDQGEMYVSP RSDNAHQIQL SKIVKQLEER
     QLNVPVLVRF PQILHQRVHS ICDAFNQAIE EYQYPNKYLL VYPIKVNQQR EVVDEILASQ
     AQLETKQLGL EAGSKPELLA VLAMAQHASS VIVCNGYKDR EYIRLALIGE KLGHKVFIVL
     EKMSELDLVL REAKSLGVTP RLGIRIRLAS QGAGKWQASG GEKSKFGLSA SQVLNVISRL
     KKENQLDTLQ LVHFHLGSQM ANIRDVRNGV NESARFYCEL RTLGANITYF DVGGGLAIDY
     DGTRSQSSNS MNYGLVEYAR NIVNTVGDVC KDYKQPMPVI ISESGRSLTA HHAVLISNVI
     GTETYKPETV TEPEEDFPLL LNNMWRSWLN LHNGTDARAL IEIYNDTQSD LAEVHSQFAT
     GVLTLEHRAW AEQTSLRIYY ELNRLMSTKN RFHRPILDEL SERLADKFFV NFSLFQSLPD
     SWGIDQVFPV LPLSGLQNAA DRRAVMLDIT CDSDGAIDAY VDGQGIESTL PVPAWNEDEP
     YLMGFFLVGA YQEILGDMHN LFGDTHSVVV NVGDQGEINI DFINEGDTVE DMMRYVHIDV
     DQIRKNYHSL VSQRVDQEEQ QQILAELEQG LSGYTYLEDF