SPEA1_SYNY3
ID SPEA1_SYNY3 Reviewed; 695 AA.
AC P74576;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Biosynthetic arginine decarboxylase 1;
DE Short=ADC 1;
DE EC=4.1.1.19;
GN Name=speA1; Synonyms=speA; OrderedLocusNames=slr0662;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine.
CC {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC SpeA subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000022; BAA18683.1; -; Genomic_DNA.
DR PIR; S76771; S76771.
DR AlphaFoldDB; P74576; -.
DR SMR; P74576; -.
DR IntAct; P74576; 2.
DR STRING; 1148.1653772; -.
DR PaxDb; P74576; -.
DR EnsemblBacteria; BAA18683; BAA18683; BAA18683.
DR KEGG; syn:slr0662; -.
DR eggNOG; COG1166; Bacteria.
DR InParanoid; P74576; -.
DR OMA; AVEYTQH; -.
DR PhylomeDB; P74576; -.
DR BRENDA; 4.1.1.19; 382.
DR Proteomes; UP000001425; Chromosome.
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; 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; 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; Reference proteome; Spermidine biosynthesis.
FT CHAIN 1..695
FT /note="Biosynthetic arginine decarboxylase 1"
FT /id="PRO_0000149981"
FT BINDING 332..342
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT MOD_RES 141
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 695 AA; 78239 MW; E90EB699D666320D CRC64;
MEGQSIELEL SVMAMPELID STEAGHTAGV KTDSNPQAIA QDRRWTIDDS ENLYRITGWG
EPYFSINAAG HVTVSPQADH GGALDLYELV KGLRQRNIGL PLLLRFSDIL ADRINRLNAA
FARGIARYRY PNTYRGVYPI KCNQHRHIVE SLVRYGTPYN FGLEAGSKPE LMIALAMLQP
QENPEPDQQN QPLLICNGYK DREYIETALL ARRLGHRPII VVEQVAEVAL AIEISSNLGI
KPILGVRAKL STQGMGRWGI STGDRAKFGL TIPEMLTAIE QLRRADMLDS LQLLHFHIGS
QISSISVIKE AMTEASQIFV QLAKLGANMR YLDVGGGLGV DYDGSKTNFY ASKNYNIQNY
VNDVISAVQD ACVAAEVPCP VLISESGRAI ASHQSVLIFD VVATNDINPP LPKVKGKDHA
ILRNLMETWE TITVDNYQEA YHDVEQFKTE AISLFNFGYL GLKERAKAEE LYWACCRKIL
QICRQQEYVP DDLENLEVNL ASIYYANMSV FQSAPDSWAI DQLFPIMPIH RLDEEPTQRG
ILADITCDSD GKIDQFIDLR DVKSVLELHP LIEVHQPGTP PRVEPYYLGM FLVGAYQEIM
GNLHNLFGDI NVVHIQMNPK GYQIEHLVRG DTIAEVLGYV QYDPEDLLEN MRRYCEQAME
DKRMSLEEAQ LLLENYERSL LQYTYLKPTS GIHTS
