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Q6HBR6 (GCSH_BACHK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. 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:
Glycine cleavage system H protein
Alternative name(s):
Octanoyl/lipoyl carrier protein
Gene names
Name:gcvH
Ordered Locus Names:BT9727_4700
OrganismBacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP]
Taxonomic identifier281309 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length127 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_00272

Is also involved in protein lipoylation via its role as an octanoyl/lipoyl carrier protein intermediate By similarity. HAMAP-Rule MF_00272

Cofactor

Binds 1 lipoyl cofactor covalently By similarity. HAMAP-Rule MF_00272

Subunit structure

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

Sequence similarities

Belongs to the GcvH family.

Contains 1 lipoyl-binding domain.

Ontologies

Keywords
   DomainLipoyl
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycine decarboxylation via glycine cleavage system

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protein lipoylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentglycine cleavage complex

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 127127Glycine cleavage system H protein HAMAP-Rule MF_00272
PRO_0000302350

Amino acid modifications

Modified residue631N6-lipoyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6HBR6 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 523CA49E2A520C14

FASTA12714,045
        10         20         30         40         50         60 
MSIPNNLRYS EEHEWVKTEG NEVVIGITHF AQNELGDIVF VELPEVGATI EADEPFGSVE 

        70         80         90        100        110        120 
SVKTVSELYA PVSGKVVAVN EELSDQPELV NESPYEGAWM VKVELSDASQ VEKLLTAEKY 


AEMTNQD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017355 Genomic DNA. Translation: AAT62561.1.
RefSeqYP_039010.1. NC_005957.1.

3D structure databases

ProteinModelPortalQ6HBR6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING281309.BT9727_4700.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT62561; AAT62561; BT9727_4700.
GeneID2853657.
KEGGbtk:BT9727_4700.
PATRIC18990602. VBIBacThu119411_4999.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0509.
HOGENOMHOG000239392.
KOK02437.
OMAADEYTAF.
OrthoDBEOG60CWTC.

Enzyme and pathway databases

BioCycBTHU281309:GJID-4791-MONOMER.

Family and domain databases

HAMAPMF_00272. GcvH.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR002930. GCV_H.
IPR017453. GCV_H_sub.
IPR011053. Single_hybrid_motif.
[Graphical view]
PANTHERPTHR11715. PTHR11715. 1 hit.
PfamPF01597. GCV_H. 1 hit.
[Graphical view]
SUPFAMSSF51230. SSF51230. 1 hit.
TIGRFAMsTIGR00527. gcvH. 1 hit.
PROSITEPS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGCSH_BACHK
AccessionPrimary (citable) accession number: Q6HBR6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 19, 2004
Last modified: May 14, 2014
This is version 66 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