ID A0A0A2TQR2_9BACL Unreviewed; 603 AA.
AC A0A0A2TQR2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Amino acid decarboxylase {ECO:0000313|EMBL:KGP78372.1};
GN ORFNames=P364_0128905 {ECO:0000313|EMBL:KGP78372.1};
OS Paenibacillus sp. MAEPY2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1395587 {ECO:0000313|EMBL:KGP78372.1, ECO:0000313|Proteomes:UP000030061};
RN [1] {ECO:0000313|EMBL:KGP78372.1, ECO:0000313|Proteomes:UP000030061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAEPY2 {ECO:0000313|EMBL:KGP78372.1,
RC ECO:0000313|Proteomes:UP000030061};
RX PubMed=24526641;
RA Chua P., Yoo H.S., Gan H.M., Lee S.M.;
RT "Draft Genome Sequences of Two Cellulolytic Paenibacillus sp. Strains,
RT MAEPY1 and MAEPY2, from Malaysian Landfill Leachate.";
RL Genome Announc. 2:0-0(2014).
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:KGP78372.1}.
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DR EMBL; AWUK01000045; KGP78372.1; -; Genomic_DNA.
DR RefSeq; WP_024633690.1; NZ_AWUK01000045.1.
DR AlphaFoldDB; A0A0A2TQR2; -.
DR eggNOG; COG1982; Bacteria.
DR OrthoDB; 9815233at2; -.
DR Proteomes; UP000030061; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR Gene3D; 3.90.1150.150; -; 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 PANTHER; PTHR43277; ARGININE DECARBOXYLASE; 1.
DR PANTHER; PTHR43277:SF3; LYSINE 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 117..469
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|Pfam:PF01276"
FT DOMAIN 529..590
FT /note="Orn/Lys/Arg decarboxylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03711"
FT REGION 44..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 603 AA; 65116 MW; 8036945DE03B856B CRC64;
MEHKSNTAPL YEALLAYRDS GQRSFHVPGH KNGQVYRRLL EQVDQQQSDR GVVDDHRNEG
EAKGKRGMGH SVHDGEECFR QAEKQRDGNE IGGLTAPDGH GSDGSAAAVV PVNAFLEMMR
LDVTEILGTD DLHHPEGAIL EAQQLAADCF GAEESFFLVG GSTSGNLSLL LTVCNEPNSL
VLVQRNVHKS VIHGLMLAGA RAVFLEPWVD PASGLAVMPS LETVQAAVQA YPEAKSVLVT
LPNYYGMGAD LTPIAEFCHA AGMPLLVDEA HGAHYGQHPE LPASALSCGA DGVVQSTHKM
LSAFTMGAML HVQGPRLNRS LLRQRLAMVQ SSSPSYPVMA SLDLARRLLH TQGANAFTAG
LAAVDAFKRG LAELPRFRLL QPAQLLQQEP PAGGKSEAAA APGRPEEVPA AALPSAAGYT
AQDPFKAVIY DGTGVLSGYG LQQQLEARGC VPEMSDERYV VLLFSLGSSL RDAEHLLQAL
RQISLEQEQS QAFDEQSQRF TKEAENYIST WNNFQEGPPF SEPIPFTLQP IMEEDTTEVS
IENSVGLRSA EMVIPYPPGI PLVYAGERIS ASMAARIKML RDEGARFHGV SDTSLQSLKI
IRE
//