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Database: UniProt
Entry: A0A934TVN2_9BURK
LinkDB: A0A934TVN2_9BURK
Original site: A0A934TVN2_9BURK 
ID   A0A934TVN2_9BURK        Unreviewed;       754 AA.
AC   A0A934TVN2;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   02-APR-2025, entry version 10.
DE   SubName: Full=Arginine/lysine/ornithine decarboxylase {ECO:0000313|EMBL:MBK6007720.1};
GN   ORFNames=JJB11_16595 {ECO:0000313|EMBL:MBK6007720.1};
OS   Ramlibacter ginsenosidimutans.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Comamonadaceae; Ramlibacter.
OX   NCBI_TaxID=502333 {ECO:0000313|EMBL:MBK6007720.1, ECO:0000313|Proteomes:UP000630528};
RN   [1] {ECO:0000313|EMBL:MBK6007720.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KACC 17527 {ECO:0000313|EMBL:MBK6007720.1};
RX   PubMed=22450785;
RA   Wang L., An D.S., Kim S.G., Jin F.X., Kim S.C., Lee S.T., Im W.T.;
RT   "Ramlibacter ginsenosidimutans sp. nov., with ginsenoside-converting
RT   activity.";
RL   J. Microbiol. Biotechnol. 22:311-315(2012).
RN   [2] {ECO:0000313|EMBL:MBK6007720.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KACC 17527 {ECO:0000313|EMBL:MBK6007720.1};
RA   Kang M.;
RL   Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
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:MBK6007720.1}.
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DR   EMBL; JAEPWM010000007; MBK6007720.1; -; Genomic_DNA.
DR   RefSeq; WP_201173759.1; NZ_JAEPWM010000007.1.
DR   Proteomes; UP000630528; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:TreeGrafter.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:TreeGrafter.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:TreeGrafter.
DR   FunFam; 3.40.640.10:FF:000008; Lysine decarboxylase, inducible; 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   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR009393-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000630528}.
FT   DOMAIN          392..406
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS00703"
FT   MOD_RES         397
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009393-1"
SQ   SEQUENCE   754 AA;  84411 MW;  BDF26BFA6413B43A CRC64;
     MKFRFPIVII DEDYRSENTS GLGIRALAEA IVAEGFEVLG VTSYGDLSQF AQQQSRASAF
     ILSIDDEEFT PGPDLDPAVL NLSNFISEVR RKNPDVPIYV YGETKTSQHL PNAILRELHG
     FIHMYEDTPE FMARHIIREA KSYLEGIQPP FFKALLDYAE DGSYSWHCPG HSGGVAFLKS
     PVGQMFHQFF GENMLRADVC NAVDELGQLL DHTGPIAASE RNAARIFNAD HCFFVTNGTS
     TSNKMVWSHE VAPGDVVVVD RNCHKSILHS IIMTGAIPVF LKPTRNHFGI IGPIPQSEFS
     PEAIKAKIKA HPLLQGVDPE TVKPRILTLT QSTYDGVLYN TETIKGLLDG YVEALHFDEA
     WIPHACFHPF YGTFHAMGKK RPRPQTSLVY STQSIHKLLA GISQASHVLV QDAVDNKLDR
     HLFNEAYLMH TSTSPQYAII ASCDVAAAMM EPPGGTALVE ESILEALDFR RAMRKVDQEY
     GKDWWFKVWG PDKLAEEGIG RADDWIIKGE ARTAKWHGFG NLAEGFNMLD PIKCTVVTPG
     LDLNGKFAKT GIPAAIVTKF LAEHGVIVEK TGLYSFFILF TIGITKGRWN TLLSALQQFK
     DDYAKNQPMW RILPEFCQQY PRYERMGLAD LCQYVHELYA KYDIAKLSTD IYLSDLQPAM
     RPSDAFAHIA HRKTDRVEID ELEGRITTAL ITPYPPGIPL LIPGEVFNKR IVEYLKFARA
     FNEECPGFET DIHGLVAEAG PDGKLRYFAD CVAQ
//
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