ID A0A136K1T7_9BACT Unreviewed; 652 AA.
AC A0A136K1T7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=arginine decarboxylase {ECO:0000256|ARBA:ARBA00012426};
DE EC=4.1.1.19 {ECO:0000256|ARBA:ARBA00012426};
GN ORFNames=UZ17_ACD001001174 {ECO:0000313|EMBL:KXK03366.1};
OS Acidobacteria bacterium OLB17.
OC Bacteria; Acidobacteriota.
OX NCBI_TaxID=1617423 {ECO:0000313|EMBL:KXK03366.1, ECO:0000313|Proteomes:UP000070331};
RN [1] {ECO:0000313|EMBL:KXK03366.1, ECO:0000313|Proteomes:UP000070331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB17 {ECO:0000313|EMBL:KXK03366.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Dutilh B.E., Jetten M.S.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine.
CC {ECO:0000256|ARBA:ARBA00002257}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR001336-50};
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC SpeA subfamily. {ECO:0000256|ARBA:ARBA00008357}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXK03366.1}.
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DR EMBL; LLEU01000025; KXK03366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136K1T7; -.
DR STRING; 1617423.UZ17_ACD001001174; -.
DR PATRIC; fig|1617423.3.peg.1224; -.
DR Proteomes; UP000070331; Unassembled WGS sequence.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
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-KW.
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 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; 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.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KXK03366.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001336-50};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066}.
FT DOMAIN 79..347
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 377..454
FT /note="Arginine decarboxylase helical bundle"
FT /evidence="ECO:0000259|Pfam:PF17810"
FT DOMAIN 588..635
FT /note="Arginine decarboxylase C-terminal helical"
FT /evidence="ECO:0000259|Pfam:PF17944"
FT ACT_SITE 505
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 99
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001336-50"
SQ SEQUENCE 652 AA; 73527 MW; D3EC16ED890B88DB CRC64;
MTAVIDKTLE TYGIDNWGAD YFGINKKGNL IVRAPENEAL TADIKEIIDD LQKRGVNAPV
LLRFPQLIFG QIRKLQVAFR KSIKEFEYEG DHLCVFPMKV NQNRSVIEEY LREGSRYNFG
LEAGSKAELY AALGLEQAKD SLLVLNGFKD REFIQLAFAG AAAGKNVVIV IEKLSELDHA
LSIADETQKA NPGMKIPMLG VRVKLYAKGS GKWEKSGGEA AKFGLTTTEI LEVIRRLQEA
GRTDLLRLLH FHIGSQLTDI KRIKNAMKEA ARTYSKIRQM GIPIEYLDVG GGMAVDYDGS
RTSFESSANY NAREFANDVI YVIKTVCDDE NVPHPTIIQE SGRYLSAYHA ILVTNVQDEI
ETVVEDLTPL NMSGNVPEVV RELHDLRETI NAKNYREYYH DALEHREELF TMFNLGLISL
EDKGAGEVLF WDICEKADGY AQMKKYVSEE FDDLRRLMCA KYLANFSVFR SMPDNWALEQ
LFPIVPIHKL NKTPTEFATF CDITCDSDGI VDKFVDLHDV KPVLELHKLV KGEPYYIAMM
LVGAYQEVMG NNHNLFGVPH EAHIFIGDDG YIIKKVIFGA TLGDAVSSVR YDAVQLHDTF
RRAVLQKIKD GDLTSKEGND LIDYYESQVD SYTYLIPHFL AAKEKKAGAA EQ
//
