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Protein

Glycine cleavage system H protein

Gene

gcvH

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.UniRule annotation

Cofactori

(R)-lipoateUniRule annotationNote: Binds 1 lipoyl cofactor covalently.UniRule annotation

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine cleavage system H proteinUniRule annotation
Gene namesi
Name:gcvHUniRule annotation
Ordered Locus Names:TM_0212
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001662581 – 124Glycine cleavage system H proteinAdd BLAST124

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei60N6-lipoyllysineUniRule annotation1

Interactioni

Subunit structurei

The glycine cleavage system is composed of four proteins: P, T, L and H.UniRule annotation

Protein-protein interaction databases

STRINGi243274.TM0212.

Structurei

Secondary structure

1124
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Beta strandi10 – 16Combined sources7
Beta strandi19 – 24Combined sources6
Helixi26 – 32Combined sources7
Beta strandi34 – 39Combined sources6
Beta strandi52 – 60Combined sources9
Beta strandi62 – 66Combined sources5
Beta strandi71 – 76Combined sources6
Helixi78 – 81Combined sources4
Helixi86 – 89Combined sources4
Turni91 – 95Combined sources5
Beta strandi98 – 103Combined sources6
Helixi105 – 110Combined sources6
Helixi114 – 122Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZKOX-ray1.65A/B1-124[»]
2KA7NMR-A1-124[»]
ProteinModelPortaliQ9WY55.
SMRiQ9WY55.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WY55.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 101Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST83

Sequence similaritiesi

Belongs to the GcvH family.UniRule annotation
Contains 1 lipoyl-binding domain.UniRule annotation

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiENOG4105KE9. Bacteria.
COG0509. LUCA.
InParanoidiQ9WY55.
KOiK02437.
OMAiNTDPYGE.

Family and domain databases

CDDicd06848. GCS_H. 1 hit.
HAMAPiMF_00272. GcvH. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR002930. GCV_H.
IPR033753. GCV_H/Fam206.
IPR017453. GCV_H_sub.
IPR011053. Single_hybrid_motif.
[Graphical view]
PANTHERiPTHR11715. PTHR11715. 1 hit.
PfamiPF01597. GCV_H. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR00527. gcvH. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9WY55-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKMKKYTKTH EWVSIEDKVA TVGITNHAQE QLGDVVYVDL PEVGREVKKG
60 70 80 90 100
EVVASIESVK AAADVYAPLS GKIVEVNEKL DTEPELINKD PEGEGWLFKM
110 120
EISDEGELED LLDEQAYQEF CAQE
Length:124
Mass (Da):13,915
Last modified:November 1, 1999 - v1
Checksum:i90B7CDE430A16C9F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35304.1.
PIRiF72403.
RefSeqiNP_228027.1. NC_000853.1.
WP_010865076.1. NC_000853.1.

Genome annotation databases

EnsemblBacteriaiAAD35304; AAD35304; TM_0212.
GeneIDi897090.
KEGGitma:TM0212.
PATRICi23935296. VBITheMar51294_0214.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35304.1.
PIRiF72403.
RefSeqiNP_228027.1. NC_000853.1.
WP_010865076.1. NC_000853.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZKOX-ray1.65A/B1-124[»]
2KA7NMR-A1-124[»]
ProteinModelPortaliQ9WY55.
SMRiQ9WY55.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM0212.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35304; AAD35304; TM_0212.
GeneIDi897090.
KEGGitma:TM0212.
PATRICi23935296. VBITheMar51294_0214.

Phylogenomic databases

eggNOGiENOG4105KE9. Bacteria.
COG0509. LUCA.
InParanoidiQ9WY55.
KOiK02437.
OMAiNTDPYGE.

Miscellaneous databases

EvolutionaryTraceiQ9WY55.

Family and domain databases

CDDicd06848. GCS_H. 1 hit.
HAMAPiMF_00272. GcvH. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR002930. GCV_H.
IPR033753. GCV_H/Fam206.
IPR017453. GCV_H_sub.
IPR011053. Single_hybrid_motif.
[Graphical view]
PANTHERiPTHR11715. PTHR11715. 1 hit.
PfamiPF01597. GCV_H. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR00527. gcvH. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGCSH_THEMA
AccessioniPrimary (citable) accession number: Q9WY55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: November 30, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.