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Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase beta chain; Aspartate 1-decarboxylase alpha chain]

 PAND_MYCTA              Reviewed;         139 AA.
A5U8S6;
02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
10-JUL-2007, sequence version 1.
16-JAN-2019, entry version 69.
RecName: Full=Aspartate 1-decarboxylase {ECO:0000255|HAMAP-Rule:MF_00446};
EC=4.1.1.11 {ECO:0000255|HAMAP-Rule:MF_00446};
AltName: Full=Aspartate alpha-decarboxylase {ECO:0000255|HAMAP-Rule:MF_00446};
Contains:
RecName: Full=Aspartate 1-decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00446};
Contains:
RecName: Full=Aspartate 1-decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00446};
Flags: Precursor;
Name=panD {ECO:0000255|HAMAP-Rule:MF_00446};
OrderedLocusNames=MRA_3640;
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=419947;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25177 / H37Ra;
PubMed=18584054; DOI=10.1371/journal.pone.0002375;
Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
Wang H., Wang S., Zhao G., Zhang Y.;
"Genetic basis of virulence attenuation revealed by comparative
genomic analysis of Mycobacterium tuberculosis strain H37Ra versus
H37Rv.";
PLoS ONE 3:E2375-E2375(2008).
[2]
FUNCTION, ACTIVITY REGULATION, POSSIBLE ANTIBIOTIC RESISTANCE, AND
MUTAGENESIS OF MET-117; 127-ASN--GLY-139; LEU-136 AND VAL-138.
STRAIN=ATCC 25177 / H37Ra;
PubMed=26038753; DOI=10.1038/emi.2014.61;
Shi W., Chen J., Feng J., Cui P., Zhang S., Weng X., Zhang W.,
Zhang Y.;
"Aspartate decarboxylase (PanD) as a new target of pyrazinamide in
Mycobacterium tuberculosis.";
Emerg. Microbes Infect. 3:E58-E58(2014).
-!- FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of
aspartate to produce beta-alanine. {ECO:0000255|HAMAP-
Rule:MF_00446}.
-!- FUNCTION: Overexpression of wild-type or mutant proteins confers
resistance to pyrazinoic acid (POA), the active form of the anti-
tuberculosis prodrug pyrazinamide (PZA), when grown on agar
plates. {ECO:0000269|PubMed:26038753}.
-!- CATALYTIC ACTIVITY:
Reaction=H(+) + L-aspartate = beta-alanine + CO2;
Xref=Rhea:RHEA:19497, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
ChEBI:CHEBI:29991, ChEBI:CHEBI:57966; EC=4.1.1.11;
Evidence={ECO:0000255|HAMAP-Rule:MF_00446};
-!- COFACTOR:
Name=pyruvate; Xref=ChEBI:CHEBI:15361;
Evidence={ECO:0000255|HAMAP-Rule:MF_00446};
Note=Binds 1 pyruvoyl group covalently per subunit.
{ECO:0000255|HAMAP-Rule:MF_00446};
-!- ACTIVITY REGULATION: Partially inhibited by POA but not by PZA or
nicotinamide, probably also inhibited by calcium pantothenate.
{ECO:0000269|PubMed:26038753}.
-!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis;
beta-alanine from L-aspartate: step 1/1. {ECO:0000255|HAMAP-
Rule:MF_00446}.
-!- SUBUNIT: Heterooctamer of four alpha and four beta subunits.
{ECO:0000255|HAMAP-Rule:MF_00446}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00446}.
-!- PTM: Is synthesized initially as an inactive proenzyme, which is
activated by self-cleavage at a specific serine bond to produce a
beta-subunit with a hydroxyl group at its C-terminus and an alpha-
subunit with a pyruvoyl group at its N-terminus.
{ECO:0000255|HAMAP-Rule:MF_00446}.
-!- MISCELLANEOUS: 30 POA or PZA-resistant mutants were identified in
this gene by selection at pH 5.7 - 6.8. The antituberculosis
activity of POA is antagonized by beta-alanine and pantothenate,
the immediate and final reaction products of this enzyme
(PubMed:26038753). Experiments in strain H37Rv suggest however
that the PZA target may not be PanD (By similarity).
{ECO:0000250|UniProtKB:P9WIL3, ECO:0000269|PubMed:26038753}.
-!- SIMILARITY: Belongs to the PanD family. {ECO:0000255|HAMAP-
Rule:MF_00446}.
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EMBL; CP000611; ABQ75426.1; -; Genomic_DNA.
RefSeq; WP_003419523.1; NZ_CP016972.1.
ProteinModelPortal; A5U8S6; -.
SMR; A5U8S6; -.
STRING; 419947.MtubH3_010100009274; -.
EnsemblBacteria; ABQ75426; ABQ75426; MRA_3640.
KEGG; mra:MRA_3640; -.
eggNOG; ENOG4108Z2X; Bacteria.
eggNOG; COG0853; LUCA.
HOGENOM; HOG000221007; -.
KO; K01579; -.
OMA; LYSKIHR; -.
OrthoDB; 1751990at2; -.
UniPathway; UPA00028; UER00002.
Proteomes; UP000001988; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004068; F:aspartate 1-decarboxylase activity; IEA:UniProtKB-UniRule.
GO; GO:0006523; P:alanine biosynthetic process; IEA:InterPro.
GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
CDD; cd06919; Asp_decarbox; 1.
HAMAP; MF_00446; PanD; 1.
InterPro; IPR009010; Asp_de-COase-like_dom_sf.
InterPro; IPR003190; Asp_decarbox.
PANTHER; PTHR21012; PTHR21012; 1.
Pfam; PF02261; Asp_decarbox; 1.
PIRSF; PIRSF006246; Asp_decarbox; 1.
ProDom; PD009294; Asp_decarbox; 1.
SUPFAM; SSF50692; SSF50692; 1.
TIGRFAMs; TIGR00223; panD; 1.
1: Evidence at protein level;
Antibiotic resistance; Autocatalytic cleavage; Complete proteome;
Cytoplasm; Decarboxylase; Lyase; Pantothenate biosynthesis; Pyruvate;
Schiff base; Zymogen.
CHAIN 1 24 Aspartate 1-decarboxylase beta chain.
{ECO:0000255|HAMAP-Rule:MF_00446}.
/FTId=PRO_0000307029.
CHAIN 25 139 Aspartate 1-decarboxylase alpha chain.
{ECO:0000255|HAMAP-Rule:MF_00446}.
/FTId=PRO_0000307030.
REGION 73 75 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_00446}.
ACT_SITE 25 25 Schiff-base intermediate with substrate;
via pyruvic acid. {ECO:0000255|HAMAP-
Rule:MF_00446}.
ACT_SITE 58 58 Proton donor. {ECO:0000255|HAMAP-
Rule:MF_00446}.
BINDING 57 57 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00446}.
MOD_RES 25 25 Pyruvic acid (Ser). {ECO:0000255|HAMAP-
Rule:MF_00446}.
MUTAGEN 117 117 M->I: Confers POA resistance, partially
inhibited by POA; identified in 24/30
mutants. {ECO:0000269|PubMed:26038753}.
MUTAGEN 127 139 Missing: Confers POA resistance.
{ECO:0000269|PubMed:26038753}.
MUTAGEN 136 136 L->R: Confers POA resistance.
{ECO:0000269|PubMed:26038753}.
MUTAGEN 138 138 V->A,E,G: Confers POA resistance.
{ECO:0000269|PubMed:26038753}.
SEQUENCE 139 AA; 14885 MW; C5BFDC1C996ED9C6 CRC64;
MLRTMLKSKI HRATVTCADL HYVGSVTIDA DLMDAADLLE GEQVTIVDID NGARLVTYAI
TGERGSGVIG INGAAAHLVH PGDLVILIAY ATMDDARART YQPRIVFVDA YNKPIDMGHD
PAFVPENAGE LLDPRLGVG


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Pathways :
WP1614: 1- and 2-Methylnaphthalene degradation
WP104: Alanine and aspartate metabolism
WP106: Alanine and aspartate metabolism
WP1493: Carbon assimilation C4 pathway
WP1518: Aspartate Biosynthesis
WP1617: Alanine, aspartate and glutamate metabolism
WP1621: Arginine and proline metabolism
WP1627: Benzoate degradation via hydroxylation
WP2185: Purine metabolism
WP240: Alanine and aspartate metabolism
WP1224: EBV LMP1 signaling
WP1225: estrogen signalling
WP1434: Osteopontin Signaling
WP1566: Citrate cycle (TCA cycle)
WP1571: EBV LMP1 signaling
WP1655: Geraniol degradation
WP1835: Interferon alpha/beta signaling
WP1904: RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways
WP210: Cytoplasmic Ribosomal Proteins
WP215: noncanonical wnt pathway
WP219: Cytoplasmic tRNA Synthetases
WP244: Alpha 6 Beta 4 signaling pathway
WP262: EBV LMP1 signaling
WP32: Translation Factors
WP433: tRNA Synthetases

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[panD MRA_3640] Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase beta chain; Aspartate 1-decarboxylase alpha chain]
[panD coaX] Multifunctional fusion protein [Cleaved into: Aspartate 1-decarboxylase alpha chain; Aspartate 1-decarboxylase beta chain] [Includes: Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase); Type III pantothenate kinase (EC 2.7.1.33) (PanK-III) (Pantothenic acid kinase)]
[Gadl1] Acidic amino acid decarboxylase GADL1 (Aspartate 1-decarboxylase) (ADC) (EC 4.1.1.11) (Cysteine sulfinic acid decarboxylase) (CSADC) (EC 4.1.1.29) (Glutamate decarboxylase-like protein 1)
[GADL1] Acidic amino acid decarboxylase GADL1 (Aspartate 1-decarboxylase) (ADC) (HuADC) (EC 4.1.1.11) (Cysteine sulfinic acid decarboxylase) (CSADC) (HuCSADC) (EC 4.1.1.29) (Glutamate decarboxylase-like protein 1)
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[psd b4160 JW4121] Phosphatidylserine decarboxylase proenzyme (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase alpha chain; Phosphatidylserine decarboxylase beta chain]
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[PKH_072580] Phosphatidylserine decarboxylase proenzyme (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase beta chain; Phosphatidylserine decarboxylase alpha chain]
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[panD HPHPP16_1572] Multifunctional fusion protein [Cleaved into: Aspartate 1-decarboxylase alpha chain; Aspartate 1-decarboxylase beta chain] [Includes: Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase); Nucleoid-associated protein HPHPP16_1572]
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[panD MSMEG_0021 MSMEI_0023] Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase beta chain; Aspartate 1-decarboxylase alpha chain]
[Got1] Aspartate aminotransferase, cytoplasmic (cAspAT) (EC 2.6.1.1) (EC 2.6.1.3) (Cysteine aminotransferase, cytoplasmic) (Cysteine transaminase, cytoplasmic) (cCAT) (Glutamate oxaloacetate transaminase 1) (Transaminase A)
[kgd Rv1248c] Multifunctional 2-oxoglutarate metabolism enzyme (2-hydroxy-3-oxoadipate synthase) (HOA synthase) (HOAS) (EC 2.2.1.5) (2-oxoglutarate carboxy-lyase) (2-oxoglutarate decarboxylase) (Alpha-ketoglutarate decarboxylase) (KG decarboxylase) (KGD) (EC 4.1.1.71) (Alpha-ketoglutarate-glyoxylate carboligase) [Includes: 2-oxoglutarate dehydrogenase E1 component (ODH E1 component) (EC 1.2.4.2) (Alpha-ketoglutarate dehydrogenase E1 component) (KDH E1 component); Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex E2 component) (ODH E2 component) (OGDC-E2) (Dihydrolipoamide succinyltransferase)]
[panD OR16_09479] Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase alpha chain; Aspartate 1-decarboxylase beta chain]
[panD OR37_01453] Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase alpha chain; Aspartate 1-decarboxylase beta chain]
[panD OR214_03545] Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase alpha chain; Aspartate 1-decarboxylase beta chain]
[panD HPHPP1_0246] Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase alpha chain; Aspartate 1-decarboxylase beta chain]
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[panD ATE51_03626 NCTC11366_01762] Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase alpha chain; Aspartate 1-decarboxylase beta chain]
[panD HPHPP11_0066] Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase alpha chain; Aspartate 1-decarboxylase beta chain]
[panD HPHPH11_0254] Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase alpha chain; Aspartate 1-decarboxylase beta chain]
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[panD Loa_00607] Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase alpha chain; Aspartate 1-decarboxylase beta chain]
[panD GY22_12620] Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase alpha chain; Aspartate 1-decarboxylase beta chain]
[panD OR16_00615] Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase alpha chain; Aspartate 1-decarboxylase beta chain]
[panD HPHPA4_0128] Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase alpha chain; Aspartate 1-decarboxylase beta chain]
[panD HPHPP4_0236] Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase alpha chain; Aspartate 1-decarboxylase beta chain]
[panD HPHPH4_0125] Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase alpha chain; Aspartate 1-decarboxylase beta chain]
[GOT1] Aspartate aminotransferase, cytoplasmic (cAspAT) (EC 2.6.1.1) (EC 2.6.1.3) (Cysteine aminotransferase, cytoplasmic) (Cysteine transaminase, cytoplasmic) (cCAT) (Glutamate oxaloacetate transaminase 1) (Transaminase A)

Bibliography :
[9169598] Escherichia coli L-aspartate-alpha-decarboxylase: preprotein processing and observation of reaction intermediates by electrospray mass spectrometry.