Q2YK15 (Q2YK15_BRUA2) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Bacterial extracellular solute-binding protein, family 3:Pyridoxal-dependent decarboxylase EMBL CAJ13031.1
EC=4.1.1.15 EMBL CAJ13031.1

Gene names

Ordered Locus Names:

BAB2_0865

Organism

Brucella abortus (strain 2308) [Complete proteome] [HAMAP]

Taxonomic identifier

359391 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella abortus

Protein attributes

Sequence length	304 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Cofactor	Pyridoxal phosphate By similarity. RuleBase RU000382
Sequence similarities	Belongs to the group II decarboxylase family. RuleBase RU000382

Ontologies

Keywords
Ligand	Pyridoxal phosphate RuleBase RU000382
Molecular function	Lyase RuleBase RU000382 EMBL CAJ13031.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	glutamate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	glutamate decarboxylase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q2YK15 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: BAE4D3D1C11CB69F	FASTA	304	34,178
	10 20 30 40 50 60 MCWHKFARYW DVEIREIPME PGRLFMGPEQ MLEAVDENTI GVVPTFGVTY TGNYEFPEPL 70 80 90 100 110 120 QDALDKLQKT KGLDIDIHVD AASGGFLAPF CAPDIPWDFR LPRVKSISAS GHKYGLAPLG 130 140 150 160 170 180 CGWVVWRDKE ALPEELIFNV DYLGGQVGTF AINFSRPAGQ VISQYYEFMR LGREGYTKVQ 190 200 210 220 230 240 QAAYRVAQYI AREIEPLGPY EFICAGEEKG GIPAVCFRIR EGEDPGYSLY DLSERLRLTG 250 260 270 280 290 300 WQVPAFALSG KASDITVMRV MCRCGFEMDL AALFIRDFKA GIEFFKSHPS PKITPSMGTG FHHT

References

[1]

"Whole-genome analyses of speciation events in pathogenic Brucellae." Microbial Genomics Group, Lawrence Livermore National Laboratory, and the Genome Analysis Group, Oak Ridge National Laboratory Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E. Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 2308.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM040265 Genomic DNA. Translation: CAJ13031.1.
RefSeq	YP_419019.1. NC_007624.1.
3D structure databases
ProteinModelPortal	Q2YK15.
SMR	Q2YK15. Positions 1-289.
ModBase	Search...
Protein-protein interaction databases
STRING	359391.BAB2_0865.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAJ13031; CAJ13031; BAB2_0865.
GeneID	3827368.
KEGG	bmf:BAB2_0865.
PATRIC	17849278. VBIBruMel86222_3158.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0076.
HOGENOM	HOG000070228.
KO	K01580.
OMA	CRCGFEM.
ProtClustDB	CLSK538368.
Enzyme and pathway databases
BioCyc	BMEL359391:GJOQ-3117-MONOMER.
Family and domain databases
Gene3D	3.40.640.10. 1 hit.
InterPro	IPR010107. Glutamate_decarboxylase. IPR002129. PyrdxlP-dep_de-COase. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR021115. Pyridoxal-P_BS. [Graphical view]
PANTHER	PTHR11999:SF1. PTHR11999:SF1. 1 hit.
Pfam	PF00282. Pyridoxal_deC. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01788. Glu-decarb-GAD. 1 hit.
PROSITE	PS00392. DDC_GAD_HDC_YDC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q2YK15_BRUA2

Accession

Primary (citable) accession number: Q2YK15

Entry history

Integrated into UniProtKB/TrEMBL:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	May 1, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)