ID A0A0G0IM10_9BACT Unreviewed; 463 AA.
AC A0A0G0IM10;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=arginine decarboxylase {ECO:0000256|ARBA:ARBA00012426};
DE EC=4.1.1.19 {ECO:0000256|ARBA:ARBA00012426};
GN ORFNames=US74_C0024G0011 {ECO:0000313|EMBL:KKQ55697.1};
OS Parcubacteria group bacterium GW2011_GWA2_38_13.
OC Bacteria.
OX NCBI_TaxID=1618811 {ECO:0000313|EMBL:KKQ55697.1, ECO:0000313|Proteomes:UP000034626};
RN [1] {ECO:0000313|EMBL:KKQ55697.1, ECO:0000313|Proteomes:UP000034626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:PIRSR600183-50};
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:KKQ55697.1}.
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DR EMBL; LBUD01000024; KKQ55697.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0IM10; -.
DR STRING; 1618811.US74_C0024G0011; -.
DR Proteomes; UP000034626; Unassembled WGS sequence.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR002985; Arg_decrbxlase.
DR InterPro; IPR022643; De-COase2_C.
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; ARGININE DECARBOXYLASE; 1.
DR PANTHER; PTHR43295:SF9; BIOSYNTHETIC ARGININE DECARBOXYLASE; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR Pfam; PF00278; Orn_DAP_Arg_deC; 1.
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};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR600183-50};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066}.
FT DOMAIN 88..315
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 317..391
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 384
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 96
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 463 AA; 52857 MW; 34D9AF9D4931F8B6 CRC64;
MKKKNKDLIN RKKFWKIGIS DFNTQYFDFN KDGELIVKEG NNQYNVRYLA EKLGTPLEIF
FPFILEERVE DLLDLTSALI KKNHYGGKFY YHYPMKVNQN KEVVMSLVGE GANLETGSYN
ELWLVKRMLE QESFNPKIRV ICNGPKTDKY INLIDDLQHR GLKVIPVIEG PNELKVFRYS
RYSVGIRLDI PVKVQSRWDK AVDRFGFSAE EILSLGKMKN LKLLHYHIGS QIELLSDILN
PIKYALDVFF KLKKINPSLD TLDIGGGMPI PYNRVKGYSV NSLMAQILKL MKTEADKRGM
PHPDLRCEWG RYIVAPSQIT VYKVIDVKNV PPKAGRAKKW YVIDGSFMND LLDTWAIHQK
WHVIPCTDKP DAKAVKVWLA GSSCDSDDIY TGQGSSIVLP DHEGNGGQGR LYLAFLDSGA
YQDPLASHHC LLSSPLKAIA ENGQIIVIRR RETPDDVGKL FGW
//
