ID A0A0G0QH29_9BACT Unreviewed; 468 AA.
AC A0A0G0QH29;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=arginine decarboxylase {ECO:0000256|ARBA:ARBA00012426};
DE EC=4.1.1.19 {ECO:0000256|ARBA:ARBA00012426};
GN ORFNames=UT74_C0012G0004 {ECO:0000313|EMBL:KKR39473.1};
OS Parcubacteria group bacterium GW2011_GWC1_40_11.
OC Bacteria.
OX NCBI_TaxID=1618902 {ECO:0000313|EMBL:KKR39473.1, ECO:0000313|Proteomes:UP000033988};
RN [1] {ECO:0000313|EMBL:KKR39473.1, ECO:0000313|Proteomes:UP000033988}
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:KKR39473.1}.
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DR EMBL; LBXY01000012; KKR39473.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0QH29; -.
DR Proteomes; UP000033988; 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:SF1; ARGININE DECARBOXYLASE 1-RELATED; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR Pfam; PF00278; Orn_DAP_Arg_deC; 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};
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 89..320
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 321..418
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT ACT_SITE 386
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 101
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
SQ SEQUENCE 468 AA; 53499 MW; 62F6433A7929D04D CRC64;
MAKTKTQKRK KIQKNWKKFW KLGAEEFNTQ YFDLSRDGEL TATEGHHVYN INDIAQKYGT
PLQIVFPFII EDRLKDLIGY FQAYIKIYGY KGKFFYHYPM KVNQNKEFIL SLLSEGANLE
ATSANELWLV KKLWEGEKFN SKIRVLCNGP KTDQYLDLIE ELRGKGMNIV PIIESLDEVD
RLSKYKGDIG VRVDLDIKTD SHWDKKFDRF GLSEKDALNL SKMKNLKIMH YHMGSQIKTQ
KSIFEGVKYG FNIYTQLQKI HPSLDTLDIG GGFGVPYEKK KFYTAKGVSS KIVKILKNLS
DKAGIRHPNL VVEWGQYIVA PAEITVYKVL SEKLIPKANA KAWYVVDGSF QNDIKDTWAI
HQKFHTIPAN NMQSPLKTTW LAGSTCDSDD KYTAGGNYIL LPKLHENQNQ FVAVLDTGAY
QDALASHHCL LSAPIKVLAQ DGTVKIVRKR ETADYIGRLF GWTNGAQN
//
