SPEA_MARN8
ID SPEA_MARN8 Reviewed; 637 AA.
AC A1TY02;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Maqu_0520;
OS Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS aquaeolei).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=351348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX PubMed=21335390; DOI=10.1128/aem.01866-10;
RA Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA Edwards K.J.;
RT "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT 'opportunitroph'.";
RL Appl. Environ. Microbiol. 77:2763-2771(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 -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC agmatine from L-arginine: step 1/1. {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; CP000514; ABM17621.1; -; Genomic_DNA.
DR RefSeq; WP_011784065.1; NC_008740.1.
DR AlphaFoldDB; A1TY02; -.
DR SMR; A1TY02; -.
DR STRING; 351348.Maqu_0520; -.
DR PRIDE; A1TY02; -.
DR EnsemblBacteria; ABM17621; ABM17621; Maqu_0520.
DR KEGG; maq:Maqu_0520; -.
DR eggNOG; COG1166; Bacteria.
DR HOGENOM; CLU_027243_1_0_6; -.
DR OMA; AVEYTQH; -.
DR OrthoDB; 164471at2; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000000998; Chromosome.
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; IPR022653; De-COase2_pyr-phos_BS.
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; SSF50621; SSF50621; 1.
DR SUPFAM; SSF51419; SSF51419; 1.
DR TIGRFAMs; TIGR01273; speA; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Magnesium; Metal-binding; Polyamine biosynthesis;
KW Pyridoxal phosphate; Spermidine biosynthesis.
FT CHAIN 1..637
FT /note="Biosynthetic arginine decarboxylase"
FT /id="PRO_1000024257"
FT BINDING 286..296
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT MOD_RES 101
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ SEQUENCE 637 AA; 70502 MW; 0D871076F7FD711C CRC64;
MAETAASPAH KVYNIAHWSD GYISVNGQGE VEICPDRGRS DARINLPALT RSLAEAGVPL
PVLIRFTDIL HDRVNKLCNA FNKVTQEQGY RGRYTAVYPI KVNQQRRVVE ELLSAEPAAS
ANQVGLEAGS KPELMAVLAL AKQAGSVIVC NGYKDREYIR LALIGQKLGH RVFIVVEKQS
ELPLILEEAK KLGISPLIGV RARLATIGKG NWQNTGGEKS KFGLSASQVL DVVDTLKQAG
ALGTLQLLHF HLGSQIANIR DIQTGLRECA RFYTELHAMG APIGTVDIGG GLGVDYEGTR
SRSSCSMNYS VFEYAYNVVH VLQSECDRQG IPHPDLISES GRALTAHHSV LVTNVIDREY
PDNREPTEPA AEAPAPLQDL WRDLESLQDE DSPRSLAEIY HDILHAMADV HAQFAHGLLS
LQERAQAETL YVRCCRMLRA ELDSANRAHR EIIDELNEKL AEKLFVNFSL FQSLPDVWGI
DQIFPVMPIN GLNRSLNRRA VIQDITCDSD GRIDQYVDGQ GIETTLPLPE HDPESPLLMG
FFMTGAYQEI LGDMHNLFGD THSVDVKLDQ QGQYQVGEPI TGDTVAKVLR YVNFEPANLL
EAYRQKFRHS GLSEELQQTL LAELSSGLEG YTYLEEG
