ID I2B3T0_SHIBC Unreviewed; 756 AA.
AC I2B3T0; K6VZI9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Biodegradative arginine decarboxylase {ECO:0000313|EMBL:AFJ45184.1};
GN OrderedLocusNames=EBL_c00470 {ECO:0000313|EMBL:AFJ45184.1};
OS Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 /
OS CDC 9005-74) (Escherichia blattae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shimwellia.
OX NCBI_TaxID=630626 {ECO:0000313|EMBL:AFJ45184.1, ECO:0000313|Proteomes:UP000001955};
RN [1] {ECO:0000313|EMBL:AFJ45184.1, ECO:0000313|Proteomes:UP000001955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74
RC {ECO:0000313|Proteomes:UP000001955};
RX PubMed=22843577; DOI=10.1128/JB.00829-12;
RA Brzuszkiewicz E., Waschkowitz T., Wiezer A., Daniel R.;
RT "Complete genome sequence of the B12-producing Shimwellia blattae strain
RT DSM 4481, isolated from a cockroach.";
RL J. Bacteriol. 194:4436-4436(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}.
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DR EMBL; CP001560; AFJ45184.1; -; Genomic_DNA.
DR RefSeq; WP_002440785.1; NZ_BAHA01000007.1.
DR AlphaFoldDB; I2B3T0; -.
DR STRING; 630626.EBL_c00470; -.
DR KEGG; ebt:EBL_c00470; -.
DR PATRIC; fig|630626.3.peg.50; -.
DR eggNOG; COG1982; Bacteria.
DR HOGENOM; CLU_014292_3_0_6; -.
DR OrthoDB; 9761189at2; -.
DR Proteomes; UP000001955; Chromosome.
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 CDD; cd00615; Orn_deC_like; 1.
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:UP000001955}.
FT DOMAIN 382..396
FT /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT attachment site"
FT /evidence="ECO:0000259|PROSITE:PS00703"
FT MOD_RES 387
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ SEQUENCE 756 AA; 84384 MW; C74529F45CB22A70 CRC64;
MCDKEYLVVG GSVAKNTPLE ECVDQIVTTL TNKGEHIRFA PTYEQATGYV SSTAAVDCVM
AEWAPHKKDD ILVFLKQFRI RHAKAPVFLL VKSHEDNKAI VPEIMSQITE TFLILDDTTD
FIVGRLQAAV ARYEKAIMPP LMAAMMKYAK EKEYSWSAPG HQGGIGFCKT PVGRKFFDFY
GENIFRTDMG IERASLGSML DHTGAFGESE KYIADVFGAD RSYSLVVGTS GSNRTIMQAC
CTDKDIAIVD RNSHKSIEQG LMLTGITPVY LTPTRNAYGI IGPIPKKQMA AQYINAAIKN
SPFASKAANQ RPVYSVITNC TYDGLIYNGD TIQALLGEST DRIHYDEAWF GYSRFNPIYK
GFHAMRGEKA SHSKDQPTIF ATHSTHKLLN ALSQASYIHI REGRGNVKPA QFNQAYMMHA
TTSPLYSIAA SNDVAAAMMD GEQGLNLTTE VIQEAVEFRQ EVARAYHAAE KNGDWFFKPW
NAEVVRCPKT GEQYDFADAP LELLTREQSC WRLQPGDSWH GFDNLDEDWV MLDPVKVSLL
APGLNDDGSL QEKGVPAALV TAYLSSIGIV PTRTTDFQIM FLFSMGVTKG KWVTLMNSLL
AFKRHYDNND LLSEVMPALV EAAPELYRGM RMQELGNRMI DFLRQYKPSE QLNKAYSTLP
AIDMLPRAAN IELVNDNVEM VSIENLAGRT AANSVIPYPP GIPMLMSGEN FGDHTSPQIA
YLKALQEWDR QFPGFEHETE GTEKEDGVYH VMCIKR
//
