ID A0A1G8IFH2_9RHOO Unreviewed; 748 AA.
AC A0A1G8IFH2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:SDI17666.1};
GN ORFNames=SAMN05660652_02978 {ECO:0000313|EMBL:SDI17666.1};
OS Propionivibrio dicarboxylicus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Propionivibrio.
OX NCBI_TaxID=83767 {ECO:0000313|EMBL:SDI17666.1, ECO:0000313|Proteomes:UP000198607};
RN [1] {ECO:0000313|EMBL:SDI17666.1, ECO:0000313|Proteomes:UP000198607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5885 {ECO:0000313|EMBL:SDI17666.1,
RC ECO:0000313|Proteomes:UP000198607};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC {ECO:0000256|ARBA:ARBA00010671}.
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DR EMBL; FNCY01000014; SDI17666.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8IFH2; -.
DR STRING; 83767.SAMN05660652_02978; -.
DR OrthoDB; 9761189at2; -.
DR Proteomes; UP000198607; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.90.100.10; Orn/Lys/Arg decarboxylase, C-terminal domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005308; OKR_de-COase_N.
DR InterPro; IPR011193; Orn/lys/arg_de-COase.
DR InterPro; IPR000310; Orn/Lys/Arg_deCO2ase_major_dom.
DR InterPro; IPR008286; Prn/Lys/Arg_de-COase_C.
DR InterPro; IPR036633; Prn/Lys/Arg_de-COase_C_sf.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR45229:SF3; BIODEGRADATIVE ARGININE DECARBOXYLASE; 1.
DR PANTHER; PTHR45229; CONSTITUTIVE ORNITHINE DECARBOXYLASE; 1.
DR Pfam; PF01276; OKR_DC_1; 1.
DR Pfam; PF03711; OKR_DC_1_C; 1.
DR Pfam; PF03709; OKR_DC_1_N; 1.
DR PIRSF; PIRSF009393; Orn_decarb; 1.
DR SUPFAM; SSF55904; Ornithine decarboxylase C-terminal domain; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00703; OKR_DC_1; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR009393-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198607}.
FT DOMAIN 388..402
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|PROSITE:PS00703"
FT MOD_RES 393
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ SEQUENCE 748 AA; 84552 MW; 3D6CF479419C9BF1 CRC64;
MRFNFPVIII DEDFRSENAS GLGIRALAEA IEKEGMEVIG VTSYGDLSSF AQQQSRASAF
ILSIDDEEFS GDQTQKTIDE LRAFVMEIRC RNEDIPIFLH GETRTSRHIP NDVLRELHGF
IHMFEDTPEF ISRYVVREAK TYLRSVPPPF FRALTHYAAD GSYSWHCPGH SGGVAFLKSP
VGQMFHQFFG ENMLRADVCN AVEELGQLLD HTGPVAASER NAARIFNADH LFFVTNGTST
SNKVVWNSTV APGDVVIVDR NCHKSVLHSI IMTGAIPVFL MPTRNHFGII GPIPKDEFRW
ENIERKIAAH PFARDVKAKP RVLTITQSTY DGILYNVEEI KEMLDGRIDT LHFDEAWLPH
AAFHDFYGDY HAIGEDRPRC KESMVFATQS THKLLAGLSQ ASQILVQNSE ARELDRAIFN
EAYLMHTSTS PQYAIIASCD VAAAMMEAPA GTALVEESIA EALDFRRAMR KVDEEWGADW
WFKVWGPDDL SEEGIEEREA WMLKPGERWH GFGQLSDGFN MLDPIKATII TPGLDVDGDF
ADGAGIPAAI VTKYLAEHGV IVEKCGLYSF FIMFTIGITK GRWNTMVTEL QQFKDDYDKN
QPLWKVLPEF VAKHPVYERM GLRDLCHLIH GVYSQNDVAR LTTEMYLSDM VPAMKPTDAF
AKMAHREIDR VPIDELEGRI TSILLTPYPP GIPLLIPGER FNATIVRYLK FARFFNEQFP
GFETDIHGLV KEVVDGKARY YVDCVRQA
//
