ID K9YFG4_HALP7 Unreviewed; 672 AA.
AC K9YFG4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 69.
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 OrderedLocusNames=PCC7418_3090 {ECO:0000313|EMBL:AFZ45212.1};
OS Halothece sp. (strain PCC 7418) (Synechococcus sp. (strain PCC 7418)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Halothecacae; Halothece cluster; Halothece.
OX NCBI_TaxID=65093 {ECO:0000313|EMBL:AFZ45212.1, ECO:0000313|Proteomes:UP000010481};
RN [1] {ECO:0000313|Proteomes:UP000010481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7418 {ECO:0000313|Proteomes:UP000010481};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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}.
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DR EMBL; CP003945; AFZ45212.1; -; Genomic_DNA.
DR RefSeq; WP_015227084.1; NC_019779.1.
DR AlphaFoldDB; K9YFG4; -.
DR STRING; 65093.PCC7418_3090; -.
DR KEGG; hao:PCC7418_3090; -.
DR PATRIC; fig|65093.3.peg.3266; -.
DR eggNOG; COG1166; Bacteria.
DR HOGENOM; CLU_027243_1_0_3; -.
DR OrthoDB; 9802658at2; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000010481; 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; 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; 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 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; PS00878; ODR_DC_2_1; 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};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01417,
KW ECO:0000256|PIRSR:PIRSR001336-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000010481};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066, ECO:0000256|HAMAP-
KW Rule:MF_01417}.
FT DOMAIN 115..373
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 398..478
FT /note="Arginine decarboxylase helical bundle"
FT /evidence="ECO:0000259|Pfam:PF17810"
FT DOMAIN 609..662
FT /note="Arginine decarboxylase C-terminal helical"
FT /evidence="ECO:0000259|Pfam:PF17944"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 530
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT BINDING 313..323
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01417"
FT MOD_RES 123
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01417,
FT ECO:0000256|PIRSR:PIRSR001336-50"
SQ SEQUENCE 672 AA; 76172 MW; DC37D429F607745A CRC64;
MSVQPQSFSS LEQNTESENH SSSSQSWTIE DSEQTYQIQG WGDPYFSINR AGHITVSPQG
DRGTSLDLYE LVTALRKRNI GLPILIRFPE ILADRVERLY ACFDRAISRY NYQGSYRGVF
PIKCNQHRHL VESLVKCGTP HQLGLEVGSK PELMIALATL NPLQISEKEA QSSLLICNGY
KDREYIETAL LSRRLGYETI LVVEQLEELE LIQAISEELA IYPAIGIRAK LGTRGTGRWG
SSTGDRAKFG LTIWQILQAV ETLKSYNKLD CLQLLHFHIG SQVSSIRVIK EAIREAAQIY
VELTNLGANL NYLDVGGGLA VDYDGSKTQK NNASKNYNMQ NYANDIVAEV KEACDQAEIK
VPTLISESGR AIASHQGVLI FDVLGSNEPP VTPPPVIEEE EHLIIRNLWE TYALINEENY
QEYYHDAIQF KQEAISLFNF SYLSLKERAR AEQLYWACCA KVFEIIKHQE TINEELQSIA
NILTSIYYIN LSIFQSAPDH WAIDQLFPIM PIHRLNEPPS KRAILADLTC DSDGKISQFI
NPKGQKPKDF LELHPLDNNQ PYYLGMFLVG AYQEIMGNLH NLFGDTNVVH IRTHGKGYKI
EQLVRGDTIT EVLAQTQYSS EELLENLRRH TEQALEKNLI SLAESRRLLN NYQQGLANYT
YLKANDQESC IP
//
