Q982G0 (PAND2_RHILO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartate 1-decarboxylase 2
EC=4.1.1.11

Alternative name(s):
Aspartate alpha-decarboxylase 2

Cleaved into the following 2 chains:

1. Aspartate 1-decarboxylase beta chain
2. Aspartate 1-decarboxylase alpha chain

Gene names

Name:	panD2
Ordered Locus Names:	mll9093

Encoded on

Plasmid pMLa

Organism

Rhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]

Taxonomic identifier

266835 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Phyllobacteriaceae › Mesorhizobium

Protein attributes

Sequence length	150 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine By similarity. HAMAP MF_00446
Catalytic activity	L-aspartate = beta-alanine + CO2. HAMAP MF_00446
Cofactor	Pyruvoyl group By similarity. HAMAP MF_00446
Pathway	Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. HAMAP MF_00446
Subunit structure	Heterooctamer of four alpha and four beta subunits By similarity.
Subcellular location	Cytoplasm By similarity HAMAP MF_00446.
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 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 Plasmid
Gene Ontology (GO)
Biological process	alanine biosynthetic process Inferred from electronic annotation. Source: InterPro pantothenate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aspartate 1-decarboxylase activity Inferred from electronic annotation. Source: EC binding Inferred from electronic annotation. Source: InterPro
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_0000023145
	Chain	24 – 150	127	Aspartate 1-decarboxylase alpha chain By similarity		PRO_0000023146
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) HAMAP MF_00446

Sequences

	Sequence		Length	Mass (Da)
	Q982G0 [UniParc]. Last modified September 26, 2001. Version 1. Checksum: EA2CA8BE680130C4	FASTA	150	16,432
	10 20 30 40 50 60 MRKIVAGKLH GIHVTEANLD YHGSITLDPD HCEEAGILPM EFVEIWNKNS GARISTYVIL 70 80 90 100 110 120 GERGSRCCIL NGAAARTCQP GDQIIVCNSI YLDEAHITSL KPRIVTFDQD NNILDRLSYS 130 140 150 VDLDPDGRYC FSILDEADEA LAIPALVSGA

References

[1]

"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti." Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S. DNA Res. 7:331-338(2000) [PubMed: 11214968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MAFF303099.

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Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000013 Genomic DNA. Translation: BAB54499.1.
RefSeq	NP_085658.1. NC_002679.1.
3D structure databases
ProteinModelPortal	Q982G0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1231545.
GenomeReviews	Gene locus mll9093 in contig BA000013_GR.
KEGG	mlo:mll9093.
NMPDR	fig|266835.1.peg.6812.
PATRIC	22488102. VBIMesLot2464_6920.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG302821.
OMA	ERSTIPV.
ProtClustDB	PRK05449.
Family and domain databases
HAMAP	MF_00446. PanD. [Tree]
InterPro	IPR009010. Asp_de-COase-like_fold. IPR003190. Asp_decarbox. [Graphical view]
Gene3D	G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit.
KO	K01579.
PANTHER	PTHR21012. Asp_decarbox. 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

PAND2_RHILO

Accession

Primary (citable) accession number: Q982G0

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	September 26, 2001
Last modified:	January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program