Skip Header

Contribute Send feedback
Read comments (?) or add your own

A0L7X7 (A0L7X7_MAGSM) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 44. Feed History...

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

Names and origin

Protein namesRecommended name:
Probable glycine dehydrogenase [decarboxylating] subunit 2 HAMAP-Rule MF_00713

EC=1.4.4.2 HAMAP-Rule MF_00713
Alternative name(s):
Glycine cleavage system P-protein subunit 2 HAMAP-Rule MF_00713
Glycine decarboxylase subunit 2 HAMAP-Rule MF_00713
Gene names
Name:gcvPB HAMAP-Rule MF_00713
Ordered Locus Names:Mmc1_1561 EMBL ABK44070.1
OrganismMagnetococcus sp. (strain MC-1) [Complete proteome] [HAMAP] EMBL ABK44070.1
Taxonomic identifier156889 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaMagnetococcalesMagnetococcaceaeMagnetococcus

Protein attributes

Sequence length491 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 SAAS SAAS020581

Catalytic activity

Glycine + H-protein-lipoyllysine = H-protein-S-aminomethyldihydrolipoyllysine + CO2. HAMAP-Rule MF_00713 SAAS SAAS020581

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00713 SAAS SAAS020581

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. HAMAP-Rule MF_00713 SAAS SAAS020581

Sequence similarities

Belongs to the GcvP family. C-terminal subunit subfamily. HAMAP-Rule MF_00713

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Amino acid modifications

Modified residue2701N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_00713

Sequences

Sequence LengthMass (Da)Tools
A0L7X7 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: AFE5EA30E642F462

FASTA49153,115
        10         20         30         40         50         60 
MSVIFESSTP GRINPQHATP LEADEQQAAL ADLPEALLRQ SPTGLPEVSE LEVVRHYTKL 

        70         80         90        100        110        120 
SQKNYSIDTH FYPLGSCTMK YNPRAANKVA MLPGFLGRHP LDDPHYATGL LHTLFELQEM 

       130        140        150        160        170        180 
LREITGMAAI SLAPMAGAQG EFAGVAMIRA YHDARGDSAR REILVPDASH GTNPATATMC 

       190        200        210        220        230        240 
GYVTREVPTN AQGDVDIEAL KSMVGPQTAG LMLTNPSTLG VFERSVGLIA RIIHDAGGLL 

       250        260        270        280        290        300 
YYDGANLNAI AGRVRPGEMG FDAIHINVHK TFATPHGGGG PGAGPVGVSA RLQPFLPIPR 

       310        320        330        340        350        360 
IVKQGASYAL LESADCPQSI GRMGAFGGNI GVLLRAHAYL CMIGRQGVRR VGEYATLNAN 

       370        380        390        400        410        420 
YLLARLTAAG FKPAYAERRA THEFIITLKA EADAYGLTAL NMAKRLLDYG FYAPTIYFPL 

       430        440        450        460        470        480 
LVPECLLIEP TETESPEQLD AFVAAMVAIR KEAQESPEFV KNAPYTTPVR RLDETRAARK 

       490 
PDLIWRGPLE Q 

« Hide

References

[1]"Complete sequence of Magnetococcus sp. MC-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Goodwin L.A., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC-1 EMBL ABK44070.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000471 Genomic DNA. Translation: ABK44070.1.
RefSeqYP_865476.1. NC_008576.1.

3D structure databases

ProteinModelPortalA0L7X7.
ModBaseSearch...

Protein-protein interaction databases

STRING156889.Mmc1_1561.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK44070; ABK44070; Mmc1_1561.
GeneID4484179.
KEGGmgm:Mmc1_1561.
PATRIC22429691. VBIMagSp23654_1601.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1003.
HOGENOMHOG000239368.
KOK00283.
OMARHYTRLS.
ProtClustDBPRK04366.

Enzyme and pathway databases

BioCycMSP156889:GH36-1617-MONOMER.

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. PyrdxlP-dep_Trfase_major. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA0L7X7_MAGSM
AccessionPrimary (citable) accession number: A0L7X7
Entry history
Integrated into UniProtKB/TrEMBL: December 12, 2006
Last sequence update: December 12, 2006
Last modified: May 1, 2013
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)