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Protein

Glycine cleavage system H protein

Gene

gcvH

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 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 annotation1 PublicationNote: Binds 1 lipoyl cofactor covalently.UniRule annotation1 Publication

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-549-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine cleavage system H proteinUniRule annotation
Gene namesi
Name:gcvHUniRule annotation
Ordered Locus Names:TTHA0524
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 128128Glycine cleavage system H proteinPRO_0000302458Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei63 – 631N6-lipoyllysineUniRule annotation1 Publication

Interactioni

Subunit structurei

The glycine cleavage system is composed of four proteins: P, T, L and H (By similarity). Monomer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi300852.TTHA0524.

Structurei

Secondary structure

1
128
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Beta strandi13 – 197Combined sources
Beta strandi22 – 276Combined sources
Helixi29 – 357Combined sources
Beta strandi37 – 426Combined sources
Beta strandi55 – 6915Combined sources
Beta strandi71 – 799Combined sources
Helixi82 – 854Combined sources
Helixi89 – 924Combined sources
Turni94 – 985Combined sources
Beta strandi101 – 1066Combined sources
Helixi108 – 1136Combined sources
Helixi117 – 12610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ONLX-ray2.50A/B/C1-128[»]
ProteinModelPortaliQ5SKW9.
SMRiQ5SKW9. Positions 2-128.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SKW9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 10483Lipoyl-bindingPROSITE-ProRule annotationAdd
BLAST

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.
HOGENOMiHOG000239392.
KOiK02437.
OMAiNTDPYGE.
PhylomeDBiQ5SKW9.

Family and domain databases

HAMAPiMF_00272. GcvH. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR002930. GCV_H.
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.

Q5SKW9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDIPKDRFYT KTHEWALPEG DTVLVGITDY AQDALGDVVY VELPEVGRVV
60 70 80 90 100
EKGEAVAVVE SVKTASDIYA PVAGEIVEVN LALEKTPELV NQDPYGEGWI
110 120
FRLKPRDMGD LDELLDAGGY QEVLESEA
Length:128
Mass (Da):14,083
Last modified:December 21, 2004 - v1
Checksum:i9A93A6CA42B4DD4E
GO

Mass spectrometryi

Molecular mass is 14083 Da from positions 1 - 128. Determined by MALDI. Unlipoylated protein.1 Publication
Molecular mass is 14273 Da from positions 1 - 128. Determined by MALDI. Lipoylated protein.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70347.1.
RefSeqiWP_011228002.1. NC_006461.1.
YP_143790.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70347; BAD70347; BAD70347.
GeneIDi3169107.
KEGGittj:TTHA0524.
PATRICi23956023. VBITheThe93045_0522.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70347.1.
RefSeqiWP_011228002.1. NC_006461.1.
YP_143790.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ONLX-ray2.50A/B/C1-128[»]
ProteinModelPortaliQ5SKW9.
SMRiQ5SKW9. Positions 2-128.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0524.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70347; BAD70347; BAD70347.
GeneIDi3169107.
KEGGittj:TTHA0524.
PATRICi23956023. VBITheThe93045_0522.

Phylogenomic databases

eggNOGiENOG4105KE9. Bacteria.
COG0509. LUCA.
HOGENOMiHOG000239392.
KOiK02437.
OMAiNTDPYGE.
PhylomeDBiQ5SKW9.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-549-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SKW9.

Family and domain databases

HAMAPiMF_00272. GcvH. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR002930. GCV_H.
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_THET8
AccessioniPrimary (citable) accession number: Q5SKW9
Secondary accession number(s): P83697
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: December 21, 2004
Last modified: September 7, 2016
This is version 80 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.