PAND_ECOLW
ID PAND_ECOLW Reviewed; 126 AA.
AC P0C7I4; E0IYQ0; H9XX93;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Aspartate 1-decarboxylase;
DE EC=4.1.1.11;
DE AltName: Full=Aspartate alpha-decarboxylase;
DE Contains:
DE RecName: Full=Aspartate 1-decarboxylase beta chain;
DE Contains:
DE RecName: Full=Aspartate 1-decarboxylase alpha chain;
DE Flags: Precursor;
GN Name=panD; OrderedLocusNames=ECW_m0128, WFL_00630;
GN ORFNames=EschWDRAFT_1457;
OS Escherichia coli (strain ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC
OS 13500 / NCIMB 8666 / NRRL B-766 / W).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=566546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 / NCIMB
RC 8666 / NRRL B-766 / W;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Tremaine M.,
RA Landick R., Keating D., Woyke T.J.;
RT "The draft genome of Escherichia coli W.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 / NCIMB
RC 8666 / NRRL B-766 / W;
RX PubMed=21208457; DOI=10.1186/1471-2164-12-9;
RA Archer C.T., Kim J.F., Jeong H., Park J.H., Vickers C.E., Lee S.Y.,
RA Nielsen L.K.;
RT "The genome sequence of E. coli W (ATCC 9637): comparative genome analysis
RT and an improved genome-scale reconstruction of E. coli.";
RL BMC Genomics 12:9-9(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 / NCIMB
RC 8666 / NRRL B-766 / W;
RX PubMed=22075923; DOI=10.1007/s10295-011-1052-2;
RA Turner P.C., Yomano L.P., Jarboe L.R., York S.W., Baggett C.L.,
RA Moritz B.E., Zentz E.B., Shanmugam K.T., Ingram L.O.;
RT "Optical mapping and sequencing of the Escherichia coli KO11 genome reveal
RT extensive chromosomal rearrangements, and multiple tandem copies of the
RT Zymomonas mobilis pdc and adhB genes.";
RL J. Ind. Microbiol. Biotechnol. 39:629-639(2012).
RN [4]
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 9637 / CCM 2024 / DSM 1116 / LMG 11080 / NBRC 13500 / NCIMB
RC 8666 / NRRL B-766 / W;
RX PubMed=381298; DOI=10.1016/s0021-9258(18)36052-6;
RA Williamson J.M., Brown G.M.;
RT "Purification and properties of L-aspartate-alpha-decarboxylase, an enzyme
RT that catalyzes the formation of beta-alanine in Escherichia coli.";
RL J. Biol. Chem. 254:8074-8082(1979).
RN [5]
RP MUTAGENESIS OF SER-25.
RC STRAIN=B / BL21-DE3;
RX PubMed=15033515; DOI=10.1016/j.ab.2003.11.027;
RA Kennedy J., Kealey J.T.;
RT "Tools for metabolic engineering in Escherichia coli: inactivation of panD
RT by a point mutation.";
RL Anal. Biochem. 327:91-96(2004).
CC -!- FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate
CC to produce beta-alanine. {ECO:0000269|PubMed:381298}.
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:0000269|PubMed:381298};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000269|PubMed:381298};
CC Note=Binds 1 pyruvoyl group covalently per subunit.
CC {ECO:0000269|PubMed:381298};
CC -!- ACTIVITY REGULATION: Inhibited by hydroxylamine, phenylhydrazine,
CC sodium borohydride, D-cycloserine, hydrazine, semicarbazine and
CC succinic dehydrazine. L-glutamate, succinate, oxaloacetate, L-serine,
CC L-cysteic acid, beta-hydroxy-DL-aspartate, and D-serine are competitive
CC inhibitors. {ECO:0000269|PubMed:381298}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=80 uM for L-aspartate (at pH 6.8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:381298};
CC KM=160 uM for L-aspartate (at pH 7.5) {ECO:0000269|PubMed:381298};
CC pH dependence:
CC Optimum pH is about 7.5. The reaction rates at the pH values of 6.8
CC and 8.0 are about 60% of the pH 7.5 rate.
CC {ECO:0000269|PubMed:381298};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius. The half-maximal activity
CC is reached at 26 degrees Celsius and 78 degrees Celsius.
CC {ECO:0000269|PubMed:381298};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-
CC alanine from L-aspartate: step 1/1.
CC -!- SUBUNIT: Heterooctamer of four alpha and four beta subunits.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the PanD family. {ECO:0000305}.
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DR EMBL; AEDF01000005; EFN38897.1; -; Genomic_DNA.
DR EMBL; CP002185; ADT73678.1; -; Genomic_DNA.
DR EMBL; CP002967; AFH09795.1; -; Genomic_DNA.
DR RefSeq; WP_000621515.1; NZ_WBMH01000004.1.
DR AlphaFoldDB; P0C7I4; -.
DR SMR; P0C7I4; -.
DR EnsemblBacteria; ADT73678; ADT73678; ECW_m0128.
DR GeneID; 66671580; -.
DR KEGG; ell:WFL_00630; -.
DR KEGG; elw:ECW_m0128; -.
DR PATRIC; fig|566546.30.peg.132; -.
DR HOGENOM; CLU_115305_2_1_6; -.
DR OMA; MLYSKIH; -.
DR SABIO-RK; P0C7I4; -.
DR UniPathway; UPA00028; UER00002.
DR Proteomes; UP000008525; 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 Autocatalytic cleavage; Cytoplasm; Decarboxylase; Lyase;
KW Pantothenate biosynthesis; Pyruvate; Schiff base; Zymogen.
FT CHAIN 1..24
FT /note="Aspartate 1-decarboxylase beta chain"
FT /id="PRO_0000337755"
FT CHAIN 25..126
FT /note="Aspartate 1-decarboxylase alpha chain"
FT /id="PRO_0000337756"
FT ACT_SITE 25
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT ACT_SITE 58
FT /note="Proton donor"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 73..75
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 25
FT /note="Pyruvic acid (Ser)"
FT /evidence="ECO:0000250"
FT MUTAGEN 25
FT /note="S->A: Inactive and incapable of self-cleavage."
FT /evidence="ECO:0000269|PubMed:15033515"
SQ SEQUENCE 126 AA; 13834 MW; E3169F5C2BDD5D25 CRC64;
MIRTMLQGKL HRVKVTHADL HYEGSCAIDQ DFLDAAGILE NEAIDIWNVT NGKRFSTYAI
AAERGSRIIS VNGAAAHCAS VGDIVIIASF VTMPDEEART WRPNVAYFEG DNEMKRTAKA
IPVQVA
