ID D4GJJ2_PANAM Unreviewed; 530 AA.
AC D4GJJ2;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Ddc {ECO:0000313|EMBL:ADD75802.1};
GN Name=ddc {ECO:0000313|EMBL:ADD75802.1};
GN OrderedLocusNames=PANA_0635 {ECO:0000313|EMBL:ADD75802.1};
OS Pantoea ananatis (strain LMG 20103).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=706191 {ECO:0000313|EMBL:ADD75802.1, ECO:0000313|Proteomes:UP000001702};
RN [1] {ECO:0000313|EMBL:ADD75802.1, ECO:0000313|Proteomes:UP000001702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20103 {ECO:0000313|EMBL:ADD75802.1,
RC ECO:0000313|Proteomes:UP000001702};
RX PubMed=20348253; DOI=10.1128/JB.00060-10;
RA De Maayer P., Chan W.Y., Venter S.N., Toth I.K., Birch P.R., Joubert F.,
RA Coutinho T.A.;
RT "Genome sequence of Pantoea ananatis LMG20103, the causative agent of
RT Eucalyptus blight and dieback.";
RL J. Bacteriol. 192:2936-2937(2010).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC {ECO:0000256|RuleBase:RU000382}.
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DR EMBL; CP001875; ADD75802.1; -; Genomic_DNA.
DR AlphaFoldDB; D4GJJ2; -.
DR STRING; 706191.PANA_0635; -.
DR KEGG; pam:PANA_0635; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_6; -.
DR Proteomes; UP000001702; Chromosome.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR CDD; cd06450; DOPA_deC_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.1650.10; PLP-dependent transferases; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000001702}.
FT MOD_RES 341
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 530 AA; 58584 MW; F19A8222969853C4 CRC64;
MAGRPTSLTK EQDMVLRKQN LSVPRRHLPD EVLNAQDFIF NDAQIPAWHQ QTQEALALIS
STVQRVEKPF SGILPHELAP AFSAVDLDQP LGNNEAALEE LRTLYLRDAV WFHHPKYVAH
LNCPVVLPSL LAEQIMAAVN SSVDTWDQSA GGTLIEQKVI DWTLGRIGLP ASADGIFTSG
GTQSNLMAML LARDSWCAAH HPGHLIKHQG LPADAAKWRV LTSRLSHFSI QKSMAILGLG
YDAVIPVAYD DHYRMDSVQL EQEIQRCHEQ GLIPIAVVAT SGTTDFGSID PLESIAKLCQ
QHGIWMHVDA AYGCGLLVSE QHRQRLNGIE KADSVTVDYH KSFFQTVSCG AFFVREKQHL
SHVTHHADYL NPLSAQQEGT PNLVNKSIQT TRRFDALKMW LTLRIMGPSA LGEAFDTILT
LTQATHQRLN AHPAIEVLHA PELTTQIFRF VPRPGMNPAQ LDAINAGIRK ALFRSGNAVI
AGTKVEGRQY LKFTLLNPTT SVADIEDVIA LIAHYGREQA RDVTLPVANQ
//
