ID H3SPR6_9BACL Unreviewed; 491 AA.
AC H3SPR6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Orn/Lys/Arg decarboxylase major region {ECO:0000313|EMBL:EHQ58937.1};
GN ORFNames=PDENDC454_27868 {ECO:0000313|EMBL:EHQ58937.1};
OS Paenibacillus dendritiformis C454.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ58937.1, ECO:0000313|Proteomes:UP000003900};
RN [1] {ECO:0000313|EMBL:EHQ58937.1, ECO:0000313|Proteomes:UP000003900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C454 {ECO:0000313|EMBL:EHQ58937.1,
RC ECO:0000313|Proteomes:UP000003900};
RX PubMed=22461558; DOI=10.1128/JB.00158-12;
RA Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., Nikolaev V.,
RA Gutnick D.L., Lancet D., Ben-Jacob E.;
RT "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT dendritiformis C454 Chiral Morphotype.";
RL J. Bacteriol. 194:2127-2128(2012).
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:EHQ58937.1}.
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DR EMBL; AHKH01000189; EHQ58937.1; -; Genomic_DNA.
DR RefSeq; WP_006680038.1; NZ_AHKH01000189.1.
DR AlphaFoldDB; H3SPR6; -.
DR STRING; 1131935.PDENDC454_27868; -.
DR PATRIC; fig|1131935.3.peg.5770; -.
DR OrthoDB; 9815233at2; -.
DR Proteomes; UP000003900; 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:UP000003900}.
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; 54005 MW; FCFF90D4F2B760A3 CRC64;
MNHHRTPLFT ALKEHAARNP VQFHIPGHKK GAGSDAEFRD FLGDNAFSID LINIAPLDDL
HQPTAVIAEA QALAADAFGA DYTYFSVQGT SGAIITMIMS VCSPGDKIIV PRNIHKSIMT
AIIFAGARPV FVSPARDANL GIDHGITTRS VRRALEKHPD AKAVLVINPT YFGICANLKE
IVDLAHSYDV PVLVDEAHGV LIHFHEKLPI SAMEAGADMA ATSVHKLGGS MTQSSVLNIN
VKNGLVNPYR VQTIFSMLTT TSTSYLLLAS LDTSRRNLAL NGHAIAERTI ELAEEARVQI
NTIPGLYCFG EDILGGEATY DFDPTKLTIH VRHLGITGYE TENWLRDHYQ LEVELSDMYN
ILCLVTPGDS KETIATLLDA LRELSATHFE KNEVQELIVK IPEIPQLSLI PRDAFYADTE
VVPFKESAGR IIAEFIYVYP PGIPILLPGE VISQQNIDYI RDHVDIGLPV KGPEDRNIEY
VKVIVEETAI F
//
