(data stored in ACNUC7421 zone)

HOGENOM: DICZE_1_PE1005

ID   DICZE_1_PE1005                       STANDARD;      PRT;   126 AA.
AC   DICZE_1_PE1005; C6CNH7;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Aspartate 1-decarboxylase; EC=4.1.1 11;AltName:
DE   Full=Aspartate alpha-decarboxylase; (DICZE_1.PE1005).
GN   Name=panD; OrderedLocusNames=Dd1591_1026;
OS   DICKEYA ZEAE ECH1591.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Dickeya.
OX   NCBI_TaxID=561229;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DICZE_1.PE1005.
CC       Dickeya zeae Ech1591 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C6CNH7_DICZE
CC   -!- FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of
CC       aspartate to produce beta-alanine (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-aspartate = beta-alanine + CO(2).
CC   -!- COFACTOR: Pyruvoyl group (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis;
CC       beta-alanine from L-aspartate: step 1/1.
CC   -!- SUBUNIT: Heterooctamer of four alpha and four beta subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Is synthesized initially as an inactive proenzyme, which is
CC       activated by self-cleavage at a specific serine bond to produce a
CC       beta-subunit with a hydroxyl group at its C-terminus and an alpha-
CC       subunit with a pyruvoyl group at its N-terminus (By similarity).
CC   -!- SIMILARITY: Belongs to the panD family.
CC   -!- GENE_FAMILY: HOG000221007 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C6CNH7; -.
DR   EMBL; CP001655; ACT05899.1; -; Genomic_DNA.
DR   RefSeq; YP_003003378.1; NC_012912.1.
DR   STRING; C6CNH7; -.
DR   GeneID; 8120299; -.
DR   GenomeReviews; CP001655_GR; Dd1591_1026.
DR   KEGG; dze:Dd1591_1026; -.
DR   OMA; LYSKIHR; -.
DR   ProtClustDB; PRK05449; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004068; F:aspartate 1-decarboxylase activity; IEA:HAMAP.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0006523; P:alanine biosynthetic process; IEA:InterPro.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00446; PanD; 1; -.
DR   InterPro; IPR009010; Asp_de-COase-like_fold.
DR   InterPro; IPR003190; Asp_decarbox.
DR   Gene3D; G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1.
DR   PANTHER; PTHR21012; Asp_decarbox; 1.
DR   Pfam; PF02261; Asp_decarbox; 1.
DR   PIRSF; PIRSF006246; Asp_decarbox; 1.
DR   ProDom; PD009294; Asp_decarbox; 1.
DR   SUPFAM; SSF50692; Asp_decarb_fold; 1.
DR   TIGRFAMs; TIGR00223; PanD; 1.
DR   HOGENOMDNA; DICZE_1.PE1005; -.
KW   Autocatalytic cleavage; Complete proteome; Cytoplasm; Decarboxylase;
KW   Lyase; Pantothenate biosynthesis; Pyruvate; Schiff base; Zymogen.
SQ   SEQUENCE   126 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MIRTMLQGKL HRVKVTQADL HYEGSCAIDQ DFMDAAGILE YEAIDIYNVD NGHRFSTYAI
     AAERGSRIIS VNGAAARCAC VGDKLIICSY VQMPDEQART HHPKVAYFGD NNELQRTAKA
     IPVQIA
//

If you have problems or comments...

PBIL Back to PBIL home page