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P65660 (PAND_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Aspartate 1-decarboxylase
EC=4.1.1.11
Alternative name(s):
Aspartate alpha-decarboxylase

Cleaved into the following 2 chains:

  1. Aspartate 1-decarboxylase beta chain
  2. Aspartate 1-decarboxylase alpha chain
Gene names
Name:panD
Ordered Locus Names:Rv3601c, MT3706.1
ORF Names:MTCY07H7B.21
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length139 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine By similarity. HAMAP-Rule MF_00446

Catalytic activity

L-aspartate = beta-alanine + CO2. HAMAP-Rule MF_00446

Cofactor

Pyruvoyl group By similarity.

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. HAMAP-Rule MF_00446

Subunit structure

Heterooctamer of four alpha and four beta subunits By similarity.

Subcellular location

Cytoplasm By similarity.

Post-translational modification

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 By similarity. HAMAP-Rule MF_00446

Sequence similarities

Belongs to the PanD family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2424Aspartate 1-decarboxylase beta chain By similarity
PRO_0000023121
Chain25 – 139115Aspartate 1-decarboxylase alpha chain By similarity
PRO_0000023122

Regions

Region73 – 753Substrate binding By similarity

Sites

Active site251Schiff-base intermediate with substrate; via pyruvic acid By similarity
Active site581Proton donor By similarity
Binding site571Substrate By similarity

Amino acid modifications

Modified residue251Pyruvic acid (Ser) By similarity

Secondary structure

1 ............................. 139
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P65660 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: C5BFDC1C996ED9C6

FASTA13914,885
        10         20         30         40         50         60 
MLRTMLKSKI HRATVTCADL HYVGSVTIDA DLMDAADLLE GEQVTIVDID NGARLVTYAI 

        70         80         90        100        110        120 
TGERGSGVIG INGAAAHLVH PGDLVILIAY ATMDDARART YQPRIVFVDA YNKPIDMGHD 

       130 
PAFVPENAGE LLDPRLGVG

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842583 Genomic DNA. Translation: CAB08943.1.
AE000516 Genomic DNA. Translation: AAK48064.1.
AL123456 Genomic DNA. Translation: CCP46424.1.
PIRB70955.
RefSeqNP_218118.1. NC_000962.3.
NP_338250.1. NC_002755.2.
YP_006517090.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C45X-ray2.99A/B/C/D/E/F/G/H1-139[»]
ProteinModelPortalP65660.
SMRP65660. Positions 1-113.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv3601c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK48064; AAK48064; MT3706.1.
GeneID13317209.
885596.
922795.
KEGGmtc:MT3706.1.
mtu:Rv3601c.
mtv:RVBD_3601c.
PATRIC18129901. VBIMycTub22151_4045.

Organism-specific databases

TubercuListRv3601c.

Phylogenomic databases

eggNOGCOG0853.
HOGENOMHOG000221007.
KOK01579.
OMALYSKIHR.
ProtClustDBPRK05449.

Enzyme and pathway databases

UniPathwayUPA00028; UER00002.

Family and domain databases

Gene3D2.40.40.20. 1 hit.
HAMAPMF_00446. PanD.
InterProIPR009010. Asp_de-COase-like_dom.
IPR003190. Asp_decarbox.
[Graphical view]
PANTHERPTHR21012. PTHR21012. 1 hit.
PfamPF02261. Asp_decarbox. 1 hit.
[Graphical view]
PIRSFPIRSF006246. Asp_decarbox. 1 hit.
ProDomPD009294. Asp_decarbox. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF50692. Asp_decarb_fold. 1 hit.
TIGRFAMsTIGR00223. panD. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP65660.

Entry information

Entry namePAND_MYCTU
AccessionPrimary (citable) accession number: P65660
Secondary accession number(s): L0TDA1, O06281
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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