Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

E8UQY4 (E8UQY4_THEBF) Unreviewed, UniProtKB/TrEMBL

Last modified March 19, 2014. Version 20. 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·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Probable glycine dehydrogenase [decarboxylating] subunit 1 HAMAP-Rule MF_00712

EC=1.4.4.2 HAMAP-Rule MF_00712
Alternative name(s):
Glycine cleavage system P-protein subunit 1 HAMAP-Rule MF_00712
Glycine decarboxylase subunit 1 HAMAP-Rule MF_00712
Glycine dehydrogenase (aminomethyl-transferring) subunit 1 HAMAP-Rule MF_00712
Gene names
Name:gcvPA HAMAP-Rule MF_00712
Ordered Locus Names:Thebr_2038 EMBL ADV80554.1
OrganismThermoanaerobacter brockii subsp. finnii (strain ATCC 43586 / DSM 3389 / AKO-1) (Thermoanaerobacter finnii) [Complete proteome] [HAMAP] EMBL ADV80554.1
Taxonomic identifier509193 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeThermoanaerobacter

Protein attributes

Sequence length447 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_00712 SAAS SAAS023010

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_00712 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_00712 SAAS SAAS020581

Sequence similarities

Belongs to the GcvP family. N-terminal subunit subfamily. HAMAP-Rule MF_00712

Sequences

Sequence LengthMass (Da)Tools
E8UQY4 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: 1CCAE3993BB31B7A

FASTA44750,064
        10         20         30         40         50         60 
MFPYLPASSN DEKEMLKTIG KNSIEELFEN IPQEVRLKRP LNLGSPMSEV ELTAHIKKYA 

        70         80         90        100        110        120 
KENKSLEELT SFLGAGVYDH YIPSVVKHII SRSEFYTAYT PYQPEISQGT LQAIFEYQTM 

       130        140        150        160        170        180 
ITNLTGMEVT NASMYDGATA CAEAAIMACE NTKRKTILVS KTVNPETRKV LKTYMHFRDI 

       190        200        210        220        230        240 
QVIEIDDNEG VTDLEKLKAE IGTNTAAVIV QYPNFFGIIE DLQEIEKITH ENKAMLITYV 

       250        260        270        280        290        300 
HPIPLGVLKS PGEIGADITV GDGQSLGNGL NFGGPYLGFL ATMQKLVRKM PGRIVGQTKD 

       310        320        330        340        350        360 
VDGKRAFVLT LQAREQHIRR EKATSNICSN HSLNALTAAV YLATMGKKGI KEVAYQCTQK 

       370        380        390        400        410        420 
AHYAFSVLTA SGKYKPAFNK PFFMEFALKT DVNVDLINKK LLEKGILGGY NLHRDYDKYE 

       430        440 
NTMLLAFTEK RTKEEIDELK ALLEVIV 

« Hide

References

[1]"Complete sequence of Thermoanaerobacter brockii finnii Ako-1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Hemme C.L., Woyke T.
Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43586 / DSM 3389 / AKO-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002466 Genomic DNA. Translation: ADV80554.1.
RefSeqYP_004186937.1. NC_014964.1.

3D structure databases

ProteinModelPortalE8UQY4.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADV80554; ADV80554; Thebr_2038.
GeneID10164321.
KEGGtbo:Thebr_2038.
PATRIC47042175. VBITheBro57020_2100.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000132025.
KOK00282.

Enzyme and pathway databases

BioCycTBRO509193:GHWP-2096-MONOMER.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
HAMAPMF_00712. GcvPA.
InterProIPR020580. GDC-P_N.
IPR020581. GDC_P.
IPR023010. GDC_P_su1.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERPTHR11773. PTHR11773. 1 hit.
PfamPF02347. GDC-P. 1 hit.
[Graphical view]
PIRSFPIRSF006815. GcvPA. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Entry information

Entry nameE8UQY4_THEBF
AccessionPrimary (citable) accession number: E8UQY4
Entry history
Integrated into UniProtKB/TrEMBL: April 5, 2011
Last sequence update: April 5, 2011
Last modified: March 19, 2014
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)