ID   SPEA_VIBCH              Reviewed;         640 AA.
AC   Q9KLD1;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 108.
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=VC_A0815;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF96713.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE003853; AAF96713.1; ALT_INIT; Genomic_DNA.
DR   PIR; E82414; E82414.
DR   RefSeq; NP_233201.1; NC_002506.1.
DR   AlphaFoldDB; Q9KLD1; -.
DR   SMR; Q9KLD1; -.
DR   STRING; 243277.VC_A0815; -.
DR   PRIDE; Q9KLD1; -.
DR   DNASU; 2611850; -.
DR   EnsemblBacteria; AAF96713; AAF96713; VC_A0815.
DR   KEGG; vch:VC_A0815; -.
DR   PATRIC; fig|243277.26.peg.3435; -.
DR   eggNOG; COG1166; Bacteria.
DR   HOGENOM; CLU_027243_1_0_6; -.
DR   OMA; AVEYTQH; -.
DR   Proteomes; UP000000584; Chromosome 2.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   GO; GO:0033388; P:putrescine biosynthetic process from arginine; IBA:GO_Central.
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; Reference proteome; Spermidine biosynthesis.
FT   CHAIN           1..640
FT                   /note="Biosynthetic arginine decarboxylase"
FT                   /id="PRO_0000149983"
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;  72249 MW;  851D1CE7D6E466F9 CRC64;
     MRYDVEQPSK LDRVRADYNV HYWSQGFFGI DDQGEVYVSP RKDKAHQTQL SSIVKQLEAR
     DLNLPVLVRF PQILHQRVHN ICDAFNQAIE EYDYPNKYLL VYPIKVNQQK EVVDEILASQ
     AELEHKQLGL EAGSKPELLA VLAMAQQASS VIVCNGYKDR EYIRLALIGE KLGHKVFIVL
     EKLSELDLVL KEAKSLGVKP RLGLRIRLAS QGAGKWQSSG GEKSKFGLAA SQVLTVINRL
     KAENQLEALQ LVHFHLGSQM ANIRDVRNGV NEAVRFYCEL RELGAHIDFF DVGGGLAVDY
     DGTRSQSSNS MNYGLHEYAR NIVSTVSDVC NLYGQPRPVI ISESGRSITA HHAVLITNVI
     GTEAYSPEEI PAPGADAPML LKNMWRGFEE VQHGTDDRAL IEIYNDTQSD LSEAHSQFAT
     GVLNLEHRAW AEQLSLRIYH ELRQKMSNKN RFHRPILDEL QERLADKFFV NFSLFQSLPD
     AWGIDQVFPV LPLSGLEEMN DRRAVMLDIT CDSDGAVEQY VEGQGIESTL PVPAWTSDKP
     YLMGFFLVGA YQEILGDMHN LFGDTHSAVV NINDNGESEI AFINEGDTVE DMMRYVHIDV
     DKIRTNYRQL VSQRVAKEEQ ETVLAELELG LSGYTYLEDF