PAND_CAMJE
ID PAND_CAMJE Reviewed; 126 AA.
AC Q9PIK3; Q0PBL3;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Aspartate 1-decarboxylase {ECO:0000255|HAMAP-Rule:MF_00446};
DE EC=4.1.1.11 {ECO:0000255|HAMAP-Rule:MF_00446};
DE AltName: Full=Aspartate alpha-decarboxylase {ECO:0000255|HAMAP-Rule:MF_00446};
DE Contains:
DE RecName: Full=Aspartate 1-decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00446};
DE Contains:
DE RecName: Full=Aspartate 1-decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00446};
DE Flags: Precursor;
GN Name=panD {ECO:0000255|HAMAP-Rule:MF_00446}; OrderedLocusNames=Cj0296c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
CC -!- FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate
CC to produce beta-alanine. {ECO:0000255|HAMAP-Rule:MF_00446}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-aspartate = beta-alanine + CO2; Xref=Rhea:RHEA:19497,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991,
CC ChEBI:CHEBI:57966; EC=4.1.1.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00446};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00446};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00446};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-
CC alanine from L-aspartate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00446}.
CC -!- SUBUNIT: Heterooctamer of four alpha and four beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00446}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00446}.
CC -!- PTM: Is synthesized initially as an inactive proenzyme, which is
CC activated by self-cleavage at a specific serine bond to produce a beta-
CC subunit with a hydroxyl group at its C-terminus and an alpha-subunit
CC with a pyruvoyl group at its N-terminus. {ECO:0000255|HAMAP-
CC Rule:MF_00446}.
CC -!- SIMILARITY: Belongs to the PanD family. {ECO:0000255|HAMAP-
CC Rule:MF_00446}.
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DR EMBL; AL111168; CAL34447.1; -; Genomic_DNA.
DR PIR; D81448; D81448.
DR RefSeq; WP_002857482.1; NC_002163.1.
DR RefSeq; YP_002343734.1; NC_002163.1.
DR PDB; 3PLX; X-ray; 1.75 A; A=1-24, B=25-126.
DR PDBsum; 3PLX; -.
DR AlphaFoldDB; Q9PIK3; -.
DR SMR; Q9PIK3; -.
DR IntAct; Q9PIK3; 80.
DR STRING; 192222.Cj0296c; -.
DR PaxDb; Q9PIK3; -.
DR PRIDE; Q9PIK3; -.
DR EnsemblBacteria; CAL34447; CAL34447; Cj0296c.
DR GeneID; 904620; -.
DR KEGG; cje:Cj0296c; -.
DR PATRIC; fig|192222.6.peg.288; -.
DR eggNOG; COG0853; Bacteria.
DR HOGENOM; CLU_115305_2_0_7; -.
DR OMA; MLYSKIH; -.
DR UniPathway; UPA00028; UER00002.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004068; F:aspartate 1-decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006523; P:alanine biosynthetic process; IEA:InterPro.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06919; Asp_decarbox; 1.
DR HAMAP; MF_00446; PanD; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003190; Asp_decarbox.
DR PANTHER; PTHR21012; PTHR21012; 1.
DR Pfam; PF02261; Asp_decarbox; 1.
DR PIRSF; PIRSF006246; Asp_decarbox; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR00223; panD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Cytoplasm; Decarboxylase; Lyase;
KW Pantothenate biosynthesis; Pyruvate; Reference proteome; Schiff base;
KW Zymogen.
FT CHAIN 1..24
FT /note="Aspartate 1-decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT /id="PRO_0000023053"
FT CHAIN 25..126
FT /note="Aspartate 1-decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT /id="PRO_0000023054"
FT ACT_SITE 25
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT ACT_SITE 58
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT BINDING 72..74
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT MOD_RES 25
FT /note="Pyruvic acid (Ser)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT STRAND 2..14
FT /evidence="ECO:0007829|PDB:3PLX"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:3PLX"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:3PLX"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:3PLX"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:3PLX"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:3PLX"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:3PLX"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:3PLX"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:3PLX"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:3PLX"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:3PLX"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:3PLX"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:3PLX"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:3PLX"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3PLX"
SQ SEQUENCE 126 AA; 13974 MW; ADC5871912B2C074 CRC64;
MNITLLKSKI HRASVTEARL DYIGSISIDE KLLQASGILE YEKVQVVNVN NGARFETYTI
ATQEEGVVCL NGAAARLAEV GDKVIIMSYA DFNEEEAKTF KPKVVFVDEN NTATKITNYE
KHGAIF
