B2HJ45 (B2HJ45_MYCMM) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Aspartate 1-decarboxylase 3 HAMAP MF_00446
EC=4.1.1.11 HAMAP MF_00446

Alternative name(s):
Aspartate alpha-decarboxylase 3 HAMAP MF_00446

Gene names

Name:	panD EMBL ACC43508.1
Synonyms:	panD3 HAMAP MF_00446
Ordered Locus Names:	MMAR_5104

Organism

Mycobacterium marinum (strain ATCC BAA-535 / M) [Complete proteome] [HAMAP]

Taxonomic identifier

216594 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	143 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. PIRSR PIRSR006246-1 HAMAP MF_00446 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. PIRSR PIRSR006246-3 HAMAP MF_00446
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 PIRSR PIRSR006246-1 HAMAP MF_00446 SAAS SAAS003190 Schiff base PIRSR PIRSR006246-1 HAMAP MF_00446 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 PIRSR PIRSR006246-2 HAMAP MF_00446
Sites
	Active site	25	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity PIRSR PIRSR006246-1 HAMAP MF_00446
	Active site	58	1	Proton donor By similarity PIRSR PIRSR006246-1 HAMAP MF_00446
	Binding site	57	1	Substrate By similarity PIRSR PIRSR006246-2 HAMAP MF_00446
Amino acid modifications
	Modified residue	25	1	Pyruvic acid (Ser) By similarity PIRSR PIRSR006246-3 HAMAP MF_00446

Sequences

	Sequence		Length	Mass (Da)
	B2HJ45 [UniParc]. Last modified June 10, 2008. Version 1. Checksum: 32A3422A947ABF24	FASTA	143	15,302
	10 20 30 40 50 60 MLRTMLKSKI HRATVTQADL HYVGSVTIDA DLMDAADLLE GEQVTIVDID NGARLVTYAI 70 80 90 100 110 120 TGERGSGVIG INGAAAHLVH PGDLVILIAY GTMQDAEARA YQPRIVFVDA DNKQIDVGHD 130 140 PAFVPAFDIP GAEELLNPRI GAR

References

[1]

"Insights from the complete genome sequence of Mycobacterium marinum on the evolution of Mycobacterium tuberculosis." Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K., Lord A., Moule S. , Mungall K., Norbertczak H., Quail M.A., Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R., Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T. Genome Res. 18:729-741(2008) [PubMed: 18403782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000854 Genomic DNA. Translation: ACC43508.1.
RefSeq	YP_001853363.1. NC_010612.1.
3D structure databases
ProteinModelPortal	B2HJ45.
SMR	B2HJ45. Positions 1-113.
ModBase	Search...
Protein-protein interaction databases
STRING	B2HJ45.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000032496; EBMYCP00000030936; EBMYCG00000032491.
GeneID	6229395.
GenomeReviews	Gene locus MMAR_5104 in contig CP000854_GR.
KEGG	mmi:MMAR_5104.
PATRIC	18071621. VBIMycMar75906_5467.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000017253.
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

B2HJ45_MYCMM

Accession

Primary (citable) accession number: B2HJ45

Entry history

Integrated into UniProtKB/TrEMBL:	June 10, 2008
Last sequence update:	June 10, 2008
Last modified:	December 14, 2011
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)