B8IQG9 (PAND_METNO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	Mnod_5641

Organism

Methylobacterium nodulans (strain ORS2060 / LMG 21967) [Complete proteome] [HAMAP]

Taxonomic identifier

460265 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Methylobacteriaceae › Methylobacterium › Methylobacterium nodulans

Protein attributes

Sequence length	152 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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.

Ontologies

Keywords
Biological process	Pantothenate biosynthesis
Cellular component	Cytoplasm
Ligand	Pyruvate Schiff base
Molecular function	Decarboxylase Lyase
PTM	Autocatalytic cleavage Zymogen
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	alanine biosynthetic process Inferred from electronic annotation. Source: InterPro pantothenate biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	aspartate 1-decarboxylase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 23	23	Aspartate 1-decarboxylase beta chain By similarity		PRO_1000192011
	Chain	24 – 152	129	Aspartate 1-decarboxylase alpha chain By similarity		PRO_1000192012
Regions
	Region	72 – 74	3	Substrate binding By similarity
Sites
	Active site	24	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity
	Active site	57	1	Proton donor By similarity
	Binding site	56	1	Substrate By similarity
Amino acid modifications
	Modified residue	24	1	Pyruvic acid (Ser) By similarity

Sequences

	Sequence		Length	Mass (Da)
	B8IQG9 [UniParc]. Last modified March 3, 2009. Version 1. Checksum: C8446A8A10295D3E	FASTA	152	17,128
	10 20 30 40 50 60 MRRIVAGKLH GIYVTDANLN YHGSITLDPD HCEEAGILPM EFVEIWNKNS GARISTYVIL 70 80 90 100 110 120 GERGSRCCIL NGAAARTCQP GDQIIICNSI YIRESELPDI RPRVLTFDSD NRVLDRLEYI 130 140 150 VKFDDFGRYR FAIERARSLN HASIAGEPKT VA

References

[1]

"Complete sequence of chromosome of Methylobacterium nodulans ORS 2060." US DOE Joint Genome Institute Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J., Richardson P. Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ORS2060 / LMG 21967.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001349 Genomic DNA. Translation: ACL60481.1.
RefSeq	YP_002500784.1. NC_011894.1.
3D structure databases
ProteinModelPortal	B8IQG9.
ModBase	Search...
Protein-protein interaction databases
STRING	460265.Mnod_5641.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACL60481; ACL60481; Mnod_5641.
GeneID	7305734.
KEGG	mno:Mnod_5641.
PATRIC	22553109. VBIMetNod76414_6247.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0853.
HOGENOM	HOG000221007.
KO	K01579.
OMA	DHCEEAG.
ProtClustDB	PRK05449.
Enzyme and pathway databases
UniPathway	UPA00028; UER00002.
Family and domain databases
Gene3D	2.40.40.20. 1 hit.
HAMAP	MF_00446. PanD.
InterPro	IPR009010. Asp_de-COase-like_dom. IPR003190. Asp_decarbox. [Graphical view]
PANTHER	PTHR21012. PTHR21012. 1 hit.
Pfam	PF02261. Asp_decarbox. 1 hit. [Graphical view]
PIRSF	PIRSF006246. Asp_decarbox. 1 hit.
ProDom	PD009294. Asp_decarbox. 1 hit. [Graphical view] [Entries sharing at least one domain]
SUPFAM	SSF50692. Asp_decarb_fold. 1 hit.
TIGRFAMs	TIGR00223. panD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PAND_METNO

Accession

Primary (citable) accession number: B8IQG9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	March 3, 2009
Last modified:	May 1, 2013
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program