ID A0A0J6NKN6_9NEIS Unreviewed; 626 AA.
AC A0A0J6NKN6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Biosynthetic arginine decarboxylase {ECO:0000256|HAMAP-Rule:MF_01417};
DE Short=ADC {ECO:0000256|HAMAP-Rule:MF_01417};
DE EC=4.1.1.19 {ECO:0000256|HAMAP-Rule:MF_01417};
GN Name=speA {ECO:0000256|HAMAP-Rule:MF_01417};
GN ORFNames=VK98_15180 {ECO:0000313|EMBL:KMN81232.1};
OS Chromobacterium sp. LK11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=1628212 {ECO:0000313|EMBL:KMN81232.1, ECO:0000313|Proteomes:UP000036114};
RN [1] {ECO:0000313|EMBL:KMN81232.1, ECO:0000313|Proteomes:UP000036114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LK11 {ECO:0000313|EMBL:KMN81232.1,
RC ECO:0000313|Proteomes:UP000036114};
RA Chan X.Y.;
RT "Draft genome of Chromobacterium aquaticum LK11.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine.
CC {ECO:0000256|ARBA:ARBA00002257, ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01417};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01417};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01417, ECO:0000256|PIRSR:PIRSR001336-50};
CC -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC agmatine from L-arginine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01417}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC SpeA subfamily. {ECO:0000256|ARBA:ARBA00008357, ECO:0000256|HAMAP-
CC Rule:MF_01417}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMN81232.1}.
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DR EMBL; LDUR01000024; KMN81232.1; -; Genomic_DNA.
DR RefSeq; WP_048414831.1; NZ_LDUR01000024.1.
DR AlphaFoldDB; A0A0J6NKN6; -.
DR STRING; 1628212.VK98_15180; -.
DR PATRIC; fig|1628212.3.peg.2148; -.
DR OrthoDB; 9802658at2; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000036114; Unassembled WGS sequence.
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:0009446; P:putrescine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06830; PLPDE_III_ADC; 1.
DR Gene3D; 1.10.287.3440; -; 1.
DR Gene3D; 1.20.58.930; -; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 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; IPR022657; De-COase2_CS.
DR InterPro; IPR022644; De-COase2_N.
DR InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR NCBIfam; TIGR01273; speA; 1.
DR PANTHER; PTHR43295; ARGININE DECARBOXYLASE; 1.
DR PANTHER; PTHR43295:SF9; BIOSYNTHETIC ARGININE DECARBOXYLASE; 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; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_01417};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01417};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01417};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01417};
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|HAMAP-
KW Rule:MF_01417}; Putrescine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01417};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01417,
KW ECO:0000256|PIRSR:PIRSR001336-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000036114};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066, ECO:0000256|HAMAP-
KW Rule:MF_01417}.
FT DOMAIN 71..339
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 368..446
FT /note="Arginine decarboxylase helical bundle"
FT /evidence="ECO:0000259|Pfam:PF17810"
FT DOMAIN 575..624
FT /note="Arginine decarboxylase C-terminal helical"
FT /evidence="ECO:0000259|Pfam:PF17944"
FT ACT_SITE 497
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT BINDING 279..289
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01417"
FT MOD_RES 99
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01417,
FT ECO:0000256|PIRSR:PIRSR001336-50"
SQ SEQUENCE 626 AA; 69747 MW; DE52001694AED28B CRC64;
MAWSVADSRA LYGIRHWGAG YFDMGANGNI VVRPNVRQNK EIDLHRLVGE LSGKGLDLPL
LVRFPDILQD RVTRLCAAFD KAIAEQGYGN RYTAIYPIKV NQQEAVVKSI IATPDVSIGL
EAGSKPELMA VLALAPKGCT IVCNGYKDRD YIRLALMGER LGHQVFIVIE KESEVELVID
ESRKLGIRPN IGMRVRLSSL ASSKWADTGG EKGKFGLSAG QLISAADKLT EAGLADCVRL
MHFHMGSQIA HIGDYRSGFG EAIRYFAELR ALGLPIDHVD VGGGLGVDYD GTHSRNDSSI
NYDMDEYAHV IVSMLSEFCG ENGIPHPRIL SESGRAMTAH HAVLIMNVTD VERLPDEVPQ
VDDIAALSQP VRKLFELVQL NDDDLVTEIY YRASHYVSEV TDLYAAGRLS LKEKALAEDV
HAALCRRLHS QLQASQRSQR QVYDELTDRL ADKYFCNFSV FQSLPDTWAI DQILPITPLH
RLNEQPTRRA VLQDLTCDSD GKLKQYVDQQ SIESSLSVHE VKQGDEYLIA VFLVGAYQEI
LGDMHNLFGD TDSVNVYVRD GGELEFSGVE EHDTIEDMLR YVHLSPEDIL NRYEAKSRAA
DLSSEERSLF FAEFCRGLKQ SSYLSV
//
