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C1L2Q6 (GCSPB_LISMC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable glycine dehydrogenase (decarboxylating) subunit 2

EC=1.4.4.2
Alternative name(s):
Glycine cleavage system P-protein subunit 2
Glycine decarboxylase subunit 2
Glycine dehydrogenase (aminomethyl-transferring) subunit 2
Gene names
Name:gcvPB
Ordered Locus Names:Lm4b_01358
OrganismListeria monocytogenes serotype 4b (strain CLIP80459) [Complete proteome] [HAMAP]
Taxonomic identifier568819 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO2 is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein By similarity. HAMAP-Rule MF_00713

Catalytic activity

Glycine + [glycine-cleavage complex H protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N(6)-dihydrolipoyl-L-lysine + CO2. HAMAP-Rule MF_00713

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00713

Subunit structure

The glycine cleavage system is composed of four proteins: P, T, L and H. In this organism, the P 'protein' is a heterodimer of two subunits By similarity.

Sequence similarities

Belongs to the GcvP family. C-terminal subunit subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 488488Probable glycine dehydrogenase (decarboxylating) subunit 2 HAMAP-Rule MF_00713
PRO_1000212672

Amino acid modifications

Modified residue2741N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C1L2Q6 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: B1F2454EADDE212B

FASTA48854,186
        10         20         30         40         50         60 
MNLEETMPLV FERSIPGRIG FSLPESDVPE TKASDYFEQA YIRSVPADLP ELSELEIMRH 

        70         80         90        100        110        120 
YTNLSNHNFG VDSGFYPLGS CTMKYNPKIN EKVARFPGFA NIHPNQPESS VQGALELLYD 

       130        140        150        160        170        180 
LQTSLVEITG MDEVTLQPAA GAHGEWTGLM LIRAFHEKNG DTKRTKVIIP DSAHGTNPAS 

       190        200        210        220        230        240 
AAVAGFDVVT VKSNEKGLVD VADLKKVVGE DTAALMLTNP NTLGLFEKDI VEMAEIVHEA 

       250        260        270        280        290        300 
GGKLYYDGAN LNAIMAKVRP GDMGFDVVHL NLHKTFTGPH GGGGPGSGPI GVKKELIPFL 

       310        320        330        340        350        360 
PTPVLTKKEE GYSFDYNYPD SIGRVKPYYG NFGINVRAYT YIRTMGPDGL KLVTEYAVLN 

       370        380        390        400        410        420 
ANYMMRKLQE AYDLPFDQVC KHEFVLSGNR QKKLGVRTVD IAKRLLDHNF HPPTVYFPLI 

       430        440        450        460        470        480 
VGEAIMIEPT ETESKETLDS FIDTMLKIAK EAEENPEIVQ EAPHSTYVKR LDETRAARKP 


ILRYQKEV 

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References

[1]"Comparative genomics and transcriptomics of lineages I, II, and III strains of Listeria monocytogenes."
Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B., Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A., Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P. expand/collapse author list , Rusniok C., Buchrieser C., Goebel W., Chakraborty T.
BMC Genomics 13:144-144(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CLIP80459.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM242711 Genomic DNA. Translation: CAS05122.1.
RefSeqYP_002758058.1. NC_012488.1.

3D structure databases

ProteinModelPortalC1L2Q6.
SMRC1L2Q6. Positions 6-486.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING634178.Lm4b_01358.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAS05122; CAS05122; Lm4b_01358.
GeneID7704392.
KEGGlmc:Lm4b_01358.
PATRIC20305887. VBILisMon88360_1370.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000239368.
KOK00283.
OMAWTGLMMI.
OrthoDBEOG6HMXDX.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
HAMAPMF_00713. GcvPB.
InterProIPR020580. GDC-P_N.
IPR020581. GDC_P.
IPR023012. GDC_P_su2.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERPTHR11773. PTHR11773. 1 hit.
PfamPF02347. GDC-P. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGCSPB_LISMC
AccessionPrimary (citable) accession number: C1L2Q6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: May 14, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families