SPEA_NOSS1
ID SPEA_NOSS1 Reviewed; 679 AA.
AC Q8YRP3;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=all3401;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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}.
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DR EMBL; BA000019; BAB75100.1; -; Genomic_DNA.
DR PIR; AB2231; AB2231.
DR AlphaFoldDB; Q8YRP3; -.
DR SMR; Q8YRP3; -.
DR STRING; 103690.17132496; -.
DR EnsemblBacteria; BAB75100; BAB75100; BAB75100.
DR KEGG; ana:all3401; -.
DR eggNOG; COG1166; Bacteria.
DR OMA; AVEYTQH; -.
DR BRENDA; 4.1.1.19; 8113.
DR Proteomes; UP000002483; 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; 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..679
FT /note="Biosynthetic arginine decarboxylase"
FT /id="PRO_0000149956"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 331..341
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT MOD_RES 149
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ SEQUENCE 679 AA; 76821 MW; 7A0AABEBB9FC6482 CRC64;
MKHRGQEEMG VESTATSDEV VKVPANGNKL EGKNHKQKKL LPTNTPGDVS RVWKIEDSEA
LYRIEGWGQP YFSINAAGHV TVSPKGDRGG SLDLFELVNA LKQRSLGLPL LIRFSDILED
RIERLNACFA KAIARYNYPG VYRGVFPVKC NQQRHLIEDL VRFGRPHQFG LEAGSKPELM
IALALLDTPG SLLICNGYKD REYVETAMLS QRLGQTPIIV LEQVEEVDLV IAASHQLGIK
PILGVRAKLS TQGMGRWGTS TGDRAKFGLT IPEIIQAVDK LRDADLLDSL QLMHFHIGSQ
ISAINVIKDA IQEASRIYVE LASLGANMKY LDVGGGLGVD YDGSQTNFYA SKNYNMQNYA
NDIVAELKDT CAEKQIPVPT LISESGRAIA SHQSVLIFDV LSTSDVPRDN PEPPKEGESP
VINYLWETYQ SINKENYQEF YHDATQFKEE AISRFNLGIL RLRERAKAER LYWACCQKIL
DIIRQHDYVP DELEDLEKIM ASIYYINLSV FQSAPDCWAI DQLFPIMPIH RLDEEPTQRG
ILADLTCDSD GKIDRFIDLR DVKSVLELHP FQPGEPYYMG MFLNGAYQEI MGNLHNLFGD
TNAVHIQLTP KGYQIEHVVK GDTMSEVVSY VQYDSEDMVE NIRQRCERAL EEKRITLAES
QRLLQTYEQS LRRYTYLNS