Reviewed, UniProtKB/Swiss-Prot Q9EYU1 (PAND1_RHILO)

Names and origin

Protein names

Recommended name:
    Aspartate 1-decarboxylase 1
    EC=4.1.1.11
Alternative name(s):
    Aspartate alpha-decarboxylase 1
Cleaved into the following 2 chains:
    1- Recommended name:
            Aspartate 1-decarboxylase beta chain
    2- Recommended name:
            Aspartate 1-decarboxylase alpha chain

Gene names

Name:	panD1
Synonyms:	panD
Ordered Locus Names:	mll5826

Organism

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

Taxonomic identifier

381 [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.
Catalytic activity	L-aspartate = beta-alanine + CO2. HAMAP MF_00446
Cofactor	Pyruvoyl group By similarity.
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.
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.
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 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_0000023143
	Chain	24 – 150	127	Aspartate 1-decarboxylase alpha chain By similarity		PRO_0000023144
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
Experimental info
	Sequence conflict	112	1	H → Y in AAG47796. Ref.1
	Sequence conflict	123	1	I → L in AAG47796. Ref.1
	Sequence conflict	132	1	A → S in AAG47796. Ref.1
	Sequence conflict	138 – 142	5	DEPLV → NEALA in AAG47796. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9EYU1-1 [UniParc]. Last modified September 26, 2001. Version 2. Checksum: 2DE3784E9A1B2084	FASTA	150	16,449
	10 20 30 40 50 60 MRKLVAGKLH GIHVTEANLN YHGSITLDPD HCEAAGILPM EFVEIWNKNS GARISTYVIL 70 80 90 100 110 120 GERGSRCCIL NGAAARTCQP DDPIIVCNSI YLDEAHITSL KPRIVTFDQD NHILDRLSYS 130 140 150 VDIDTDGRYS FAILDEADEP LVIPALVSGA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Biosynthetic operons for biotin and nicotinic acid mononucleotide are present on the acquired symbiosis island of Mesorhizobium sp. strain R7A: the bio operon incudes a novel gene involved in pimeloyl-CoA synthesis." Sullivan J.T., Brown S.D., Yocum R., Ronson C.W. Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: R7A.
[2]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF311738 Genomic DNA. Translation: AAG47796.1. BA000012 Genomic DNA. Translation: BAB52207.1.
RefSeq	NP_106421.1.
3D structure databases
HSSP	HSSP built from PDB template 1AW8 based on UniProtKB P31664.
ModBase	Search...
Genome annotation databases
GeneID	1229080.
GenomeReviews	Gene locus mll5826 in contig BA000012_GR.
KEGG	mlo:mll5826.
NMPDR	fig|266835.1.peg.4524.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9EYU1.
OMA	ISTYVIF.
Enzyme and pathway databases
BRENDA	4.1.1.11. 3315.
Family and domain databases
HAMAP	MF_00446. [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.
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]
TIGRFAMs	TIGR00223. panD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PAND1_RHILO

Accession

Primary (citable) accession number: Q9EYU1
Secondary accession number(s): Q98AW5

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	September 26, 2001
Last modified:	November 3, 2009
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)