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Database: UniProt
Entry: A0A0Q5Z9C6_9BURK
LinkDB: A0A0Q5Z9C6_9BURK
Original site: A0A0Q5Z9C6_9BURK 
ID   A0A0Q5Z9C6_9BURK        Unreviewed;       755 AA.
AC   A0A0Q5Z9C6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Lysine decarboxylase {ECO:0000313|EMBL:KQT10811.1};
GN   ORFNames=ASG30_08350 {ECO:0000313|EMBL:KQT10811.1};
OS   Ramlibacter sp. Leaf400.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ramlibacter.
OX   NCBI_TaxID=1736365 {ECO:0000313|EMBL:KQT10811.1, ECO:0000313|Proteomes:UP000051173};
RN   [1] {ECO:0000313|EMBL:KQT10811.1, ECO:0000313|Proteomes:UP000051173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf400 {ECO:0000313|EMBL:KQT10811.1,
RC   ECO:0000313|Proteomes:UP000051173};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT10811.1, ECO:0000313|Proteomes:UP000051173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf400 {ECO:0000313|EMBL:KQT10811.1,
RC   ECO:0000313|Proteomes:UP000051173};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQT10811.1}.
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DR   EMBL; LMQL01000010; KQT10811.1; -; Genomic_DNA.
DR   RefSeq; WP_055896672.1; NZ_LMQL01000010.1.
DR   AlphaFoldDB; A0A0Q5Z9C6; -.
DR   STRING; 1736365.ASG30_08350; -.
DR   OrthoDB; 9761189at2; -.
DR   Proteomes; UP000051173; Unassembled WGS sequence.
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   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:UP000051173}.
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   755 AA;  84634 MW;  5F966E2DB8BE06DB CRC64;
     MKFRFPIVII DEDYRSENTS GLGIRALAQA IEAEGMEVLG ATSYGDLAQF AQQQSRASAF
     ILSIDDEEFT SGPDPDPAVL NLRNFIGEVR RKNSDVPIYL YGETKTSQHL PNDVLRELHG
     FIHMYEDTPE FMARHIIREA KSYLEGIQPP FFRALLDYAE DGSYSWHCPG HSGGVAFLKS
     PIGQMFHQFF GENMLRADVC NAVDELGQLL DHTGPVAASE RNAARIFNAD HCFFVTNGTS
     TSNKMVWHHT VAPGDVVVVD RNCHKSILHS IIMTGAIPVF MKPTRNHFGI IGPIPQSEFT
     PEAIKAKIRA NPLLAGVDPE QVKPRIMTLT QSTYDGVLYN TETIKGMLDG YVDALHFDEA
     WLPHACFHPF YGAFHAMGKK RARPEKSLVY ATQSIHKLLA GISQASHVLV QDAKNNKLDR
     HLFNEAFLMH TSTSPQYSII ASCDVAAAMM EPPGGTALVE ESIQEALDFR RAMRKVDQEY
     GKDWWFKVWG PDRLAESGIG RADDWIIKGE ARAAKWHGFG NLAEGFNMLD PIKSTVVTPG
     LDLNGKFAKT GIPASIVTRF LAEHGIIVEK TGLYSFFIMF TIGITKGRWN TLLTALQQFK
     DDYARNQPMW RILPEFCAQH PRYERMGLAD LCQHVHEMYA KYDIARLTTD MYLSDLTPAM
     KPSDAYAHIA HRKTERVEID ELEGRVTTSL VTPYPPGIPL LIPGEVFNRK IVDYLKFSRE
     FNASCPGFET DIHGLVEEVG ADGKTRYYAD CVRAS
//
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