C8X1K4 (C8X1K4_DESRD) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

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

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

Gene names

Name:	panD HAMAP-Rule MF_00446
Ordered Locus Names:	Dret_1013 EMBL ACV68301.1

Organism

Desulfohalobium retbaense (strain DSM 5692) [Complete proteome] [HAMAP] EMBL ACV68301.1

Taxonomic identifier

485915 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Deltaproteobacteria › Desulfovibrionales › Desulfohalobiaceae › Desulfohalobium › Desulfohalobium retbaense

Protein attributes

Sequence length	126 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-Rule MF_00446 SAAS SAAS003190
Catalytic activity	L-aspartate = beta-alanine + CO2. HAMAP-Rule MF_00446 SAAS SAAS003190
Cofactor	Pyruvoyl group By similarity. PIRSR PIRSR006246-1 HAMAP-Rule MF_00446 SAAS SAAS003190
Pathway	Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. HAMAP-Rule MF_00446 SAAS SAAS003190
Subunit structure	Heterooctamer of four alpha and four beta subunits By similarity. HAMAP-Rule MF_00446 SAAS SAAS003190
Subcellular location	Cytoplasm By similarity HAMAP-Rule 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-Rule MF_00446
Sequence similarities	Belongs to the PanD family. HAMAP-Rule MF_00446

Ontologies

Keywords
Biological process	Pantothenate biosynthesis HAMAP-Rule MF_00446 SAAS SAAS003190
Cellular component	Cytoplasm HAMAP-Rule MF_00446 SAAS SAAS003190
Ligand	Pyruvate PIRSR PIRSR006246-1 HAMAP-Rule MF_00446 SAAS SAAS003190 Schiff base PIRSR PIRSR006246-1 HAMAP-Rule MF_00446 SAAS SAAS003190
Molecular function	Decarboxylase HAMAP-Rule MF_00446 SAAS SAAS003190 Lyase
PTM	Autocatalytic cleavage HAMAP-Rule MF_00446 Zymogen HAMAP-Rule 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Region	72 – 74	3	Substrate binding By similarity PIRSR PIRSR006246-2 HAMAP-Rule MF_00446
Sites
	Active site	26	1	Schiff-base intermediate with substrate; via pyruvic acid By similarity PIRSR PIRSR006246-1 HAMAP-Rule MF_00446
	Active site	59	1	Proton donor By similarity PIRSR PIRSR006246-1 HAMAP-Rule MF_00446
	Binding site	58	1	Substrate By similarity PIRSR PIRSR006246-2 HAMAP-Rule MF_00446
Amino acid modifications
	Modified residue	26	1	Pyruvic acid (Ser) By similarity PIRSR PIRSR006246-3 HAMAP-Rule MF_00446

Sequences

	Sequence		Length	Mass (Da)
	C8X1K4 [UniParc]. Last modified November 3, 2009. Version 1. Checksum: C64E53BB411480C0	FASTA	126	13,275
	10 20 30 40 50 60 MALRTYLQCK LHRGTVTGAD LEYEGSISIC SQLLRCAGLH VHERVEVYNV TNGERFATYV 70 80 90 100 110 120 IPGEAGEIGV NGAAAHKASP GDQVIIAAYV QLTPEEAAGH SPDVVLLGDE NSVVRIQKGS GPCVAS

References

[1]

"The complete chromosome of Desulfohalobium retbaense DSM 5692." US DOE Joint Genome Institute (JGI-PGF) Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R. , Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Klenk H.-P., Eisen J.A. Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 5692.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001734 Genomic DNA. Translation: ACV68301.1.
RefSeq	YP_003197879.1. NC_013223.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	485915.Dret_1013.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACV68301; ACV68301; Dret_1013.
GeneID	8418836.
KEGG	drt:Dret_1013.
PATRIC	21699002. VBIDesRet71890_1084.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0853.
HOGENOM	HOG000221007.
KO	K01579.
OMA	DHCEEAG.
ProtClustDB	CLSK2556089.
Enzyme and pathway databases
BioCyc	DRET485915:GHRJ-1033-MONOMER.
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

C8X1K4_DESRD

Accession

Primary (citable) accession number: C8X1K4

Entry history

Integrated into UniProtKB/TrEMBL:	November 3, 2009
Last sequence update:	November 3, 2009
Last modified:	May 29, 2013
This is version 26 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)