PAND_HELPY
ID PAND_HELPY Reviewed; 117 AA.
AC P56065;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
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=HP_0034;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP PROTEOLYTIC PROCESSING BY SELF, PYRUVATE FORMATION AT SER-25, AND SUBUNIT.
RX PubMed=15184017; DOI=10.1016/j.jmb.2004.04.049;
RA Lee B.I., Suh S.W.;
RT "Crystal structure of the Schiff base intermediate prior to decarboxylation
RT in the catalytic cycle of aspartate alpha-decarboxylase.";
RL J. Mol. Biol. 340:1-7(2004).
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 Note=Binds 1 pyruvoyl group covalently per subunit.;
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, ECO:0000269|PubMed:15184017}.
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.
CC -!- SIMILARITY: Belongs to the PanD family. {ECO:0000255|HAMAP-
CC Rule:MF_00446}.
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DR EMBL; AE000511; AAD07103.1; -; Genomic_DNA.
DR PIR; B64524; B64524.
DR RefSeq; NP_206836.1; NC_000915.1.
DR RefSeq; WP_000142250.1; NC_018939.1.
DR PDB; 1UHD; X-ray; 2.00 A; A=26-117, B=1-24.
DR PDB; 1UHE; X-ray; 1.55 A; A=26-117, B=1-24.
DR PDBsum; 1UHD; -.
DR PDBsum; 1UHE; -.
DR AlphaFoldDB; P56065; -.
DR SMR; P56065; -.
DR STRING; 85962.C694_00160; -.
DR PaxDb; P56065; -.
DR EnsemblBacteria; AAD07103; AAD07103; HP_0034.
DR KEGG; hpy:HP_0034; -.
DR PATRIC; fig|85962.47.peg.35; -.
DR eggNOG; COG0853; Bacteria.
DR OMA; MLYSKIH; -.
DR PhylomeDB; P56065; -.
DR BRENDA; 4.1.1.11; 2604.
DR UniPathway; UPA00028; UER00002.
DR EvolutionaryTrace; P56065; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004068; F:aspartate 1-decarboxylase activity; IBA:GO_Central.
DR GO; GO:0006523; P:alanine biosynthetic process; IBA:GO_Central.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IBA:GO_Central.
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_0000023091"
FT CHAIN 25..117
FT /note="Aspartate 1-decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT /id="PRO_0000023092"
FT ACT_SITE 25
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000269|PubMed:15184017"
FT ACT_SITE 58
FT /note="Proton donor"
FT BINDING 57
FT /ligand="substrate"
FT BINDING 72..74
FT /ligand="substrate"
FT MOD_RES 25
FT /note="Pyruvic acid (Ser)"
FT /evidence="ECO:0000269|PubMed:15184017"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:1UHE"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:1UHE"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1UHE"
FT HELIX 30..35
FT /evidence="ECO:0007829|PDB:1UHE"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1UHE"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1UHE"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:1UHE"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1UHE"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1UHE"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:1UHE"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:1UHE"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:1UHE"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:1UHE"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:1UHE"
SQ SEQUENCE 117 AA; 12939 MW; 430A9A537644E4EF CRC64;
MTFEMLYSKI HRATITDANL NYIGSITIDE DLAKLAKLRE GMKVEIVDVN NGERFSTYVI
LGKKRGEICV NGAAARKVAI GDVVIILAYA SMNEDEINAH KPSIVLVDEK NEILEKG
