ID A0A0T7BWE3_9CYAN Unreviewed; 671 AA.
AC A0A0T7BWE3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 42.
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 ORFNames=IJ00_21130 {ECO:0000313|EMBL:AKG23445.1};
OS Calothrix sp. 336/3.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=1337936 {ECO:0000313|EMBL:AKG23445.1, ECO:0000313|Proteomes:UP000065745};
RN [1] {ECO:0000313|EMBL:AKG23445.1, ECO:0000313|Proteomes:UP000065745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=336/3 {ECO:0000313|EMBL:AKG23445.1,
RC ECO:0000313|Proteomes:UP000065745};
RX PubMed=25614574;
RA Isojarvi J., Shunmugam S., Sivonen K., Allahverdiyeva Y., Aro E.M.,
RA Battchikova N.;
RT "Draft genome sequence of calothrix strain 336/3, a novel h2-producing
RT cyanobacterium isolated from a finnish lake.";
RL Genome Announc. 3:0-0(2015).
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; CP011382; AKG23445.1; -; Genomic_DNA.
DR RefSeq; WP_035156408.1; NZ_CP011382.1.
DR AlphaFoldDB; A0A0T7BWE3; -.
DR STRING; 1337936.IJ00_21130; -.
DR KEGG; calh:IJ00_21130; -.
DR eggNOG; COG1166; Bacteria.
DR OrthoDB; 9802658at2; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000065745; 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; 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 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.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000065745};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066, ECO:0000256|HAMAP-
KW Rule:MF_01417}.
FT DOMAIN 133..382
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 408..489
FT /note="Arginine decarboxylase helical bundle"
FT /evidence="ECO:0000259|Pfam:PF17810"
FT DOMAIN 616..669
FT /note="Arginine decarboxylase C-terminal helical"
FT /evidence="ECO:0000259|Pfam:PF17944"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 631..662
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 539
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT BINDING 323..333
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01417"
FT MOD_RES 141
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01417,
FT ECO:0000256|PIRSR:PIRSR001336-50"
SQ SEQUENCE 671 AA; 75726 MW; BC2C93609938D2D8 CRC64;
MRVESTATSE EVVKPPSNGK KAEMKHPKHK KLLLPAASEE GSRTWKIEDS EALYRIEGWG
QPYFSINAAG HVTVSPKGDR GGSLDLFELV NALKQRNLGL PLLIRFSDIL EDRIERLNSC
FAKAIARYNY PGVYRGVFPV KCNQQRHLIE DLVRFGKPHQ FGLEAGSKPE LMIALALLDT
PGALLVCNGY KDREYIETAM LAQRLGQTPI IVLEQVEEVD LVIEVSRQLG IQPIVGVRAK
LSTQGMGRWG TSSGDRAKFG LTIPEIIQAV DKLRDANLLG SLQLLHFHVG SQISAINVIK
DAIQEASRIY VELAALGADM KYLDVGGGLG VDYDGSQTNF YASKNYNMQN YANDIVAELK
DTCTERNIAV PTLISESGRA IASHQSVLIF DVLSTSEIIA ETPEPPKEGE PPVITYLWET
YQSINDENFQ EFYHDAAQFK EEAISRFNLG ILTLTERAKA ERLYWACCHK ILSIIRKLDY
VPDELEDLEK IMASIYYVNL SVFQSAPDCW AIDQLFPIMP IHRLSEEPNR RGILADLTCD
SDGKIDRFID LRDVKSVLEL HEFQPGEPYY LGMFLNGAYQ EIMGNLHNLF GDTNAVHIQL
TPKGYQIEHV VKGDTMSEVV SYVQYDSEDM VENIRQRCEK ALEEKRITLA ESQRLLQTYE
QSLRRYTYLY P
//
