ID A0A1S2QSG2_9BACI Unreviewed; 491 AA.
AC A0A1S2QSG2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:OIK09054.1};
GN ORFNames=BIV59_18115 {ECO:0000313|EMBL:OIK09054.1};
OS Bacillus sp. MUM 13.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1678001 {ECO:0000313|EMBL:OIK09054.1, ECO:0000313|Proteomes:UP000180199};
RN [1] {ECO:0000313|EMBL:OIK09054.1, ECO:0000313|Proteomes:UP000180199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUM 13 {ECO:0000313|EMBL:OIK09054.1,
RC ECO:0000313|Proteomes:UP000180199};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Bacillus sp. MUM 13.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC {ECO:0000256|ARBA:ARBA00010671}.
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:OIK09054.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MLYQ01000088; OIK09054.1; -; Genomic_DNA.
DR RefSeq; WP_071352864.1; NZ_MLYQ01000088.1.
DR AlphaFoldDB; A0A1S2QSG2; -.
DR Proteomes; UP000180199; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd00615; Orn_deC_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
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; PTHR43277; ARGININE DECARBOXYLASE; 1.
DR PANTHER; PTHR43277:SF4; ARGININE DECARBOXYLASE; 1.
DR Pfam; PF01276; OKR_DC_1; 1.
DR Pfam; PF03711; OKR_DC_1_C; 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 Reference proteome {ECO:0000313|Proteomes:UP000180199}.
FT DOMAIN 221..235
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|PROSITE:PS00703"
SQ SEQUENCE 491 AA; 53744 MW; B157A2101C3C5F52 CRC64;
MSQYETPLFT GLINHAKKNP IQFHIPGHKK GQGIDPEFRN FIGENALSID LINIAPLDDL
HQPKGIIKQA QDLAAEAFGA DHTFFSVQGT SGAIMTMVMA VCGPGDKIIV PRNVHKSVMS
AIVFSGAVPI FIHPEIDKEL GISHGITTES VEKALEQNPD AKGLLVINPT YFGVSADLKK
IVEIAHSYSV PVLVDEAHGV HIHFHEGLPM SAMQAGADMA ATSVHKLGGS LTQSSVLNVK
EGLVSSNHVQ SILSMLTTTS TSYILLASLD VARKRLATEG RELIDKAIKL ADHIRYEVNT
IPKLTCIGRE ILGSKATFDY DPTKLIISVK ELGISGYDVE KWLREKHNIE VELSDLYNIL
CLVTTGDTET EAEILISALR DLAEEFNHYQ GENQEISEVM LPDIPLLALT PRDAFYASTE
VVPIEESAGR IIAEFIMVYP PGIPIFIPGE IITEENIAYI KKNIEVGLPV QGPEDSELKN
LRVIKERKAI I
//