PAND_ECOLI
ID PAND_ECOLI Reviewed; 126 AA.
AC P0A790; P31664; Q8KMY8;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=b0131, JW0127;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8837478; DOI=10.1111/j.1574-6968.1996.tb08488.x;
RA Merkel W.K., Nichols B.P.;
RT "Characterization and sequence of the Escherichia coli panBCD gene
RT cluster.";
RL FEMS Microbiol. Lett. 143:247-252(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 107
RP AND 120-121.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-5 AND 25-29, AND CHARACTERIZATION.
RX PubMed=9169598; DOI=10.1042/bj3230661;
RA Ramjee M.K., Genschel U., Abell C., Smith A.G.;
RT "Escherichia coli L-aspartate-alpha-decarboxylase: preprotein processing
RT and observation of reaction intermediates by electrospray mass
RT spectrometry.";
RL Biochem. J. 323:661-669(1997).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=6767707; DOI=10.1128/jb.141.3.1291-1297.1980;
RA Cronan J.E. Jr.;
RT "Beta-alanine synthesis in Escherichia coli.";
RL J. Bacteriol. 141:1291-1297(1980).
RN [7]
RP ENZYME MECHANISM.
RX PubMed=12240302; DOI=10.1039/b106090m;
RA Saldanha S.A., Birch L.M., Webb M.E., Nabbs B.K., von Delft F., Smith A.G.,
RA Abell C.;
RT "Identification of Tyr58 as the proton donor in the aspartate-alpha-
RT decarboxylase reaction.";
RL Chem. Commun. (Camb.) 18:1760-1761(2001).
RN [8]
RP ACTIVITY REGULATION, AND INTERACTION WITH PANZ.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=23170229; DOI=10.1002/mbo3.34;
RA Nozaki S., Webb M.E., Niki H.;
RT "An activator for pyruvoyl-dependent l-aspartate alpha-decarboxylase is
RT conserved in a small group of the gamma-proteobacteria including
RT Escherichia coli.";
RL MicrobiologyOpen 1:298-310(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-115, PROTEOLYTIC PROCESSING BY
RP SELF, SUBUNIT, AND PYRUVATE FORMATION AT SER-25.
RX PubMed=9546220; DOI=10.1038/nsb0498-289;
RA Albert A., Dhanaraj V., Genschel U., Khan G., Ramjee M.K., Pulido R.,
RA Sibanda B.L., von Delft F., Witty M., Blundell T.L., Smith A.G., Abell C.;
RT "Crystal structure of aspartate decarboxylase at 2.2-A resolution provides
RT evidence for an ester in protein self-processing.";
RL Nat. Struct. Biol. 5:289-293(1998).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.29 ANGSTROMS), AND PROTEOLYTIC PROCESSING BY SELF.
RX PubMed=14633979; DOI=10.1093/emboj/cdg575;
RA Schmitzberger F., Kilkenny M.L., Lobley C.M.C., Webb M.E., Vinkovic M.,
RA Matak-Vinkovic D., Witty M., Chirgadze D.Y., Smith A.G., Abell C.,
RA Blundell T.L.;
RT "Structural constraints on protein self-processing in L-aspartate-alpha-
RT decarboxylase.";
RL EMBO J. 22:6193-6204(2003).
RN [11] {ECO:0007744|PDB:4CRY}
RP X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS) OF 1-24 AND 25-126 IN COMPLEX WITH
RP PANZ AND ACETYL COENZYME A.
RA Monteiro D.C.F., Patel V., Bartlett C.P., Grant T.D., Nozaki S.,
RA Gowdy J.A., Snell E.H., Niki H., Pearson A.R., Webb M.E.;
RT "Direct visualisation of strain-induced protein post-translational
RT modification.";
RL Submitted (MAR-2014) to the PDB data bank.
RN [12] {ECO:0007744|PDB:4CRZ, ECO:0007744|PDB:4CS0}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANTS ALA-25 AND VAL-57 IN
RP COMPLEXES WITH PANZ AND ACETYL COENZYME A, ACTIVITY REGULATION, AND
RP INTERACTION WITH PANZ.
RX PubMed=25910242; DOI=10.1016/j.chembiol.2015.03.017;
RA Monteiro D.C., Patel V., Bartlett C.P., Nozaki S., Grant T.D., Gowdy J.A.,
RA Thompson G.S., Kalverda A.P., Snell E.H., Niki H., Pearson A.R., Webb M.E.;
RT "The structure of the PanD/PanZ protein complex reveals negative feedback
RT regulation of pantothenate biosynthesis by coenzyme A.";
RL Chem. Biol. 22:492-503(2015).
CC -!- FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate
CC to produce beta-alanine. {ECO:0000269|PubMed:6767707}.
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;
CC Evidence={ECO:0000269|PubMed:6767707};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Note=Binds 1 pyruvoyl group covalently per subunit.;
CC -!- ACTIVITY REGULATION: Inhibited by hydroxylamine, sodium borohydride, D-
CC cycloserine, hydrazine, semicarbazine and succinic dehydrazine
CC (PubMed:6767707). D-serine is a competitive inhibitor (PubMed:6767707).
CC Cleavage and catalytic activity are regulated by PanZ in a coenzyme A
CC (CoA)-dependent fashion (PubMed:23170229, PubMed:25910242).
CC {ECO:0000269|PubMed:23170229, ECO:0000269|PubMed:25910242,
CC ECO:0000269|PubMed:6767707}.
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 (PubMed:9546220). Interacts with PanZ (PubMed:23170229,
CC PubMed:25910242). {ECO:0000269|PubMed:23170229,
CC ECO:0000269|PubMed:25910242, ECO:0000269|PubMed:9546220}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:6767707}.
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:0000305}.
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DR EMBL; L17086; AAA24274.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73242.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96708.2; -; Genomic_DNA.
DR PIR; C64736; C64736.
DR RefSeq; NP_414673.1; NC_000913.3.
DR RefSeq; WP_000621515.1; NZ_STEB01000010.1.
DR PDB; 1AW8; X-ray; 2.20 A; A/D=1-24, B/E=25-115.
DR PDB; 1PPY; X-ray; 1.95 A; A/B=1-126.
DR PDB; 1PQE; X-ray; 1.95 A; A=1-126.
DR PDB; 1PQF; X-ray; 2.00 A; A/B=1-126.
DR PDB; 1PQH; X-ray; 1.29 A; A/B=1-126.
DR PDB; 1PT0; X-ray; 2.00 A; A/B=1-126.
DR PDB; 1PT1; X-ray; 1.90 A; A/B=1-126.
DR PDB; 1PYQ; X-ray; 1.90 A; A/B=1-126.
DR PDB; 1PYU; X-ray; 1.90 A; A/C=1-24, B/D=25-126.
DR PDB; 3TM7; X-ray; 1.70 A; A/C=1-24, B/D=25-126.
DR PDB; 4AOK; X-ray; 1.50 A; A/D=1-24, B/E=26-126.
DR PDB; 4AON; X-ray; 1.50 A; A/D=1-24, B/E=25-126.
DR PDB; 4AZD; X-ray; 1.62 A; A/B=1-126.
DR PDB; 4CRY; X-ray; 1.61 A; A=1-24, G=25-126.
DR PDB; 4CRZ; X-ray; 1.70 A; A=1-126.
DR PDB; 4CS0; X-ray; 2.10 A; A=1-126.
DR PDB; 4D7Z; X-ray; 1.90 A; A=1-24, B=26-119.
DR PDB; 5LS7; X-ray; 1.16 A; A=1-24, D=25-126.
DR PDBsum; 1AW8; -.
DR PDBsum; 1PPY; -.
DR PDBsum; 1PQE; -.
DR PDBsum; 1PQF; -.
DR PDBsum; 1PQH; -.
DR PDBsum; 1PT0; -.
DR PDBsum; 1PT1; -.
DR PDBsum; 1PYQ; -.
DR PDBsum; 1PYU; -.
DR PDBsum; 3TM7; -.
DR PDBsum; 4AOK; -.
DR PDBsum; 4AON; -.
DR PDBsum; 4AZD; -.
DR PDBsum; 4CRY; -.
DR PDBsum; 4CRZ; -.
DR PDBsum; 4CS0; -.
DR PDBsum; 4D7Z; -.
DR PDBsum; 5LS7; -.
DR AlphaFoldDB; P0A790; -.
DR SMR; P0A790; -.
DR BioGRID; 4259730; 213.
DR IntAct; P0A790; 2.
DR STRING; 511145.b0131; -.
DR PaxDb; P0A790; -.
DR PRIDE; P0A790; -.
DR EnsemblBacteria; AAC73242; AAC73242; b0131.
DR EnsemblBacteria; BAB96708; BAB96708; BAB96708.
DR GeneID; 66671580; -.
DR GeneID; 945686; -.
DR KEGG; ecj:JW0127; -.
DR KEGG; eco:b0131; -.
DR PATRIC; fig|1411691.4.peg.2151; -.
DR EchoBASE; EB1697; -.
DR eggNOG; COG0853; Bacteria.
DR HOGENOM; CLU_115305_2_1_6; -.
DR InParanoid; P0A790; -.
DR OMA; MLYSKIH; -.
DR PhylomeDB; P0A790; -.
DR BioCyc; EcoCyc:ASPDECARBOX-MON; -.
DR BioCyc; MetaCyc:ASPDECARBOX-MON; -.
DR BRENDA; 4.1.1.11; 2026.
DR SABIO-RK; P0A790; -.
DR UniPathway; UPA00028; UER00002.
DR EvolutionaryTrace; P0A790; -.
DR PRO; PR:P0A790; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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 GO; GO:0016540; P:protein autoprocessing; IDA:EcoCyc.
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;
KW Direct protein sequencing; Lyase; Pantothenate biosynthesis; Pyruvate;
KW Reference proteome; Schiff base; Zymogen.
FT CHAIN 1..24
FT /note="Aspartate 1-decarboxylase beta chain"
FT /id="PRO_0000023073"
FT CHAIN 25..126
FT /note="Aspartate 1-decarboxylase alpha chain"
FT /id="PRO_0000023074"
FT ACT_SITE 25
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000269|PubMed:9546220"
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:0000269|PubMed:9546220"
FT CONFLICT 107
FT /note="Y -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 120..121
FT /note="AI -> TV (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 2..14
FT /evidence="ECO:0007829|PDB:5LS7"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:5LS7"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:1PQH"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:5LS7"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:5LS7"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:5LS7"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:5LS7"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:5LS7"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5LS7"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:5LS7"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:5LS7"
FT STRAND 84..94
FT /evidence="ECO:0007829|PDB:5LS7"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:5LS7"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:5LS7"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:5LS7"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:5LS7"
SQ SEQUENCE 126 AA; 13834 MW; E3169F5C2BDD5D25 CRC64;
MIRTMLQGKL HRVKVTHADL HYEGSCAIDQ DFLDAAGILE NEAIDIWNVT NGKRFSTYAI
AAERGSRIIS VNGAAAHCAS VGDIVIIASF VTMPDEEART WRPNVAYFEG DNEMKRTAKA
IPVQVA
