SPEA2_SYNY3
ID SPEA2_SYNY3 Reviewed; 659 AA.
AC P72587;
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 2;
DE Short=ADC 2;
DE EC=4.1.1.19;
GN Name=speA2; Synonyms=speA; OrderedLocusNames=slr1312;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-302.
RA Mulo P., Eloranta T., Aro E.M., Maenpaeae P.;
RT "Disruption of a spe-like open reading frame alters polyamine content and
RT psbA-2 mRNA stability in the cyanobacterium Synechocystis sp. PCC 6803.";
RL Bot. Acta 111:71-76(1998).
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}.
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DR EMBL; BA000022; BAA16587.1; -; Genomic_DNA.
DR EMBL; X96602; CAA65422.1; -; Genomic_DNA.
DR PIR; S74435; S74435.
DR AlphaFoldDB; P72587; -.
DR SMR; P72587; -.
DR STRING; 1148.1651659; -.
DR PaxDb; P72587; -.
DR EnsemblBacteria; BAA16587; BAA16587; BAA16587.
DR KEGG; syn:slr1312; -.
DR eggNOG; COG1166; Bacteria.
DR InParanoid; P72587; -.
DR PhylomeDB; P72587; -.
DR BRENDA; 4.1.1.19; 6192.
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; 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.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Magnesium; Metal-binding; Polyamine biosynthesis;
KW Pyridoxal phosphate; Reference proteome; Spermidine biosynthesis.
FT CHAIN 1..659
FT /note="Biosynthetic arginine decarboxylase 2"
FT /id="PRO_0000149982"
FT BINDING 311..321
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT MOD_RES 119
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 659 AA; 74477 MW; E8442002C8CD4629 CRC64;
MGEEPVPADK ALGKKFKKKN ASWSIEESEA LYRVEAWGAP YFAINAAGNI TVSPNGDRGG
SLDLLELVEA LRQRKLGLPL LIRFSDILAD RLERLNSCFA KAIARYNYPN TYQAVYPVKC
NQQRHLVEAL VRFGQTSQCG LEAGSKPELM IALATLPPPL DRQDKHTKPL IICNGYKDQD
YLETALLAKR LGHRPIIIIE QLRELEWVLH ISQQLNIKPM LGVRARLSCQ SLKSSEISSG
NGDRAKLGLT MPDIVTVIHR LEENNCLDCL KMLHFHLGTQ VSDIALIKEA MREASQLYVE
LVKLGAKMRY LNVGGGLAVD YDGSKTNYPA SKNYNMQNYA NDIVAAIQDA CELGQVSPPI
LVSESGRAIM AHQSVLVFDV LGSNQTGFSE PHPPDENAHP LLKNLWECYE TITAEQYQEQ
YHDALQLKTE ASSLFNFGYL SLTERGQAEQ IHWACCRKIF EITRQLEYIP EDFQALDKIM
TDIYYVNLSV FQSAPESWSL DQLFPILPIH HLNEKPSQRV ILADLTCDSD GKIDRFIDLW
DVKSYLEVHP LENDGNPYYL GMFLVGAYQE IMGNLHNLFG DINVVHIATT PQGYQIESVV
RGDTMTEVLG YVQYDSDDLL EGLRRHTELA LSNGQITLEE SRRLLEDYEQ SLRRYTYLS
