A5FLR1 (A5FLR1_FLAJ1) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Aspartate 1-decarboxylase HAMAP MF_00446
EC=4.1.1.11 HAMAP MF_00446

Alternative name(s):
Aspartate alpha-decarboxylase HAMAP MF_00446

Gene names

Name:	panD HAMAP MF_00446
Ordered Locus Names:	Fjoh_0826

Organism

Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101) (Cytophaga johnsonae) [Complete proteome] [HAMAP]

Taxonomic identifier

376686 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Flavobacteriia › Flavobacteriales › Flavobacteriaceae › Flavobacterium

Protein attributes

Sequence length	116 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine By similarity. HAMAP MF_00446 SAAS SAAS003190
Catalytic activity	L-aspartate = beta-alanine + CO2. HAMAP MF_00446 SAAS SAAS003190
Cofactor	Pyruvoyl group By similarity. HAMAP MF_00446 PIRSR PIRSR006246-1 SAAS SAAS003190
Pathway	Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. HAMAP MF_00446 SAAS SAAS003190
Subunit structure	Heterooctamer of four alpha and four beta subunits By similarity. HAMAP MF_00446 SAAS SAAS003190
Subcellular location	Cytoplasm By similarity HAMAP MF_00446 SAAS SAAS003190.
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 PIRSR PIRSR006246-3
Sequence similarities	Belongs to the PanD family. HAMAP MF_00446

Ontologies

Keywords
Biological process	Pantothenate biosynthesis HAMAP MF_00446 SAAS SAAS003190
Cellular component	Cytoplasm HAMAP MF_00446 SAAS SAAS003190
Ligand	Pyruvate HAMAP MF_00446 PIRSR PIRSR006246-1 SAAS SAAS003190 Schiff base HAMAP MF_00446 PIRSR PIRSR006246-1 SAAS SAAS003190
Molecular function	Decarboxylase HAMAP MF_00446 SAAS SAAS003190 Lyase
PTM	Autocatalytic cleavage HAMAP MF_00446 Zymogen HAMAP MF_00446
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
Regions
	Region	73 – 75	3	Substrate binding By similarity HAMAP MF_00446 PIRSR PIRSR006246-2
Sites
	Active site	25	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity HAMAP MF_00446 PIRSR PIRSR006246-1
	Active site	58	1	Proton donor By similarity HAMAP MF_00446 PIRSR PIRSR006246-1
	Binding site	57	1	Substrate By similarity HAMAP MF_00446 PIRSR PIRSR006246-2
Amino acid modifications
	Modified residue	25	1	Pyruvic acid (Ser) By similarity HAMAP MF_00446 PIRSR PIRSR006246-3

Sequences

	Sequence		Length	Mass (Da)
	A5FLR1 [UniParc]. Last modified June 12, 2007. Version 1. Checksum: EF9533DB17EFFA31	FASTA	116	12,968
	10 20 30 40 50 60 MQIQVIKSKI HRVKVTGADL NYIGSITIDE TLLEASNIIE GEKVSIVNIN NGERFETYAI 70 80 90 100 110 KGEKNSGEIT LNGPAARKVQ KDDIIIIISY ATLDFEEAKT FKPWIIFPNE NDNSLT

References

[1]

"Complete sequence of Flavobacterium johnsoniae UW101." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E., Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Xie G., McBride M., Richardson P. Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 17061 / DSM 2064 / UW101.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000685 Genomic DNA. Translation: ABQ03860.1.
RefSeq	YP_001193179.1. NC_009441.1.
3D structure databases
ProteinModelPortal	A5FLR1.
ModBase	Search...
Protein-protein interaction databases
STRING	A5FLR1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5092015.
GenomeReviews	Gene locus Fjoh_0826 in contig CP000685_GR.
KEGG	fjo:Fjoh_0826.
PATRIC	21895927. VBIFlaJoh53613_0848.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0853.
HOGENOM	HBG302821.
OMA	LYSKIHR.
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

A5FLR1_FLAJ1

Accession

Primary (citable) accession number: A5FLR1

Entry history

Integrated into UniProtKB/TrEMBL:	June 12, 2007
Last sequence update:	June 12, 2007
Last modified:	December 14, 2011
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)