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Protein

Glycine cleavage system H protein

Gene

gcvH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 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.

Cofactori

(R)-lipoateNote: Binds 1 lipoyl cofactor covalently.

GO - Molecular functioni

  • lipoic acid binding Source: EcoliWiki

GO - Biological processi

  • glycine decarboxylation via glycine cleavage system Source: EcoliWiki
Complete GO annotation...

Enzyme and pathway databases

BioCyciEcoCyc:GCVH-MONOMER.
ECOL316407:JW2872-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine cleavage system H proteinUniRule annotation
Gene namesi
Name:gcvHUniRule annotation
Ordered Locus Names:b2904, JW2872
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10371. gcvH.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: EcoCyc
  • glycine cleavage complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 129128Glycine cleavage system H proteinPRO_0000166218Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651N6-lipoyllysineUniRule annotation

Proteomic databases

EPDiP0A6T9.
PaxDbiP0A6T9.
PRIDEiP0A6T9.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi4261019. 11 interactions.
IntActiP0A6T9. 2 interactions.
STRINGi511145.b2904.

Structurei

Secondary structure

1
129
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 113Combined sources
Beta strandi14 – 196Combined sources
Beta strandi25 – 295Combined sources
Helixi31 – 377Combined sources
Beta strandi39 – 446Combined sources
Beta strandi57 – 659Combined sources
Beta strandi67 – 715Combined sources
Beta strandi73 – 819Combined sources
Helixi83 – 864Combined sources
Helixi91 – 944Combined sources
Turni96 – 1005Combined sources
Beta strandi103 – 1086Combined sources
Helixi110 – 1156Combined sources
Beta strandi116 – 1183Combined sources
Helixi119 – 1279Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A7AX-ray3.10B/D2-129[»]
3A7LX-ray1.30A2-129[»]
3A8IX-ray1.99E/F1-129[»]
3A8JX-ray1.98E/F1-129[»]
3A8KX-ray1.95E/F1-129[»]
3AB9X-ray1.65A1-129[»]
ProteinModelPortaliP0A6T9.
SMRiP0A6T9. Positions 2-129.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6T9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 10683Lipoyl-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

eggNOGiCOG0509. LUCA.
HOGENOMiHOG000239392.
InParanoidiP0A6T9.
KOiK02437.
OMAiNTDPYGE.
PhylomeDBiP0A6T9.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A6T9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNVPAELKY SKEHEWLRKE ADGTYTVGIT EHAQELLGDM VFVDLPEVGA
60 70 80 90 100
TVSAGDDCAV AESVKAASDI YAPVSGEIVA VNDALSDSPE LVNSEPYAGG
110 120
WIFKIKASDE SELESLLDAT AYEALLEDE
Length:129
Mass (Da):13,811
Last modified:January 23, 2007 - v2
Checksum:i79748C818BD1325F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57690 Genomic DNA. Translation: AAA68887.1.
X73958 Genomic DNA. Translation: CAA52145.1.
U28377 Genomic DNA. Translation: AAA69072.1.
U00096 Genomic DNA. Translation: AAC75942.1.
M97263 Unassigned DNA. Translation: AAC36844.1.
L20872 Genomic DNA. Translation: AAA23866.1.
AP009048 Genomic DNA. Translation: BAE76969.1.
PIRiA56623.
RefSeqiNP_417380.1. NC_000913.3.
WP_001295377.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75942; AAC75942; b2904.
BAE76969; BAE76969; BAE76969.
GeneIDi947393.
KEGGiecj:JW2872.
eco:b2904.
PATRICi32121222. VBIEscCol129921_2999.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57690 Genomic DNA. Translation: AAA68887.1.
X73958 Genomic DNA. Translation: CAA52145.1.
U28377 Genomic DNA. Translation: AAA69072.1.
U00096 Genomic DNA. Translation: AAC75942.1.
M97263 Unassigned DNA. Translation: AAC36844.1.
L20872 Genomic DNA. Translation: AAA23866.1.
AP009048 Genomic DNA. Translation: BAE76969.1.
PIRiA56623.
RefSeqiNP_417380.1. NC_000913.3.
WP_001295377.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A7AX-ray3.10B/D2-129[»]
3A7LX-ray1.30A2-129[»]
3A8IX-ray1.99E/F1-129[»]
3A8JX-ray1.98E/F1-129[»]
3A8KX-ray1.95E/F1-129[»]
3AB9X-ray1.65A1-129[»]
ProteinModelPortaliP0A6T9.
SMRiP0A6T9. Positions 2-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261019. 11 interactions.
IntActiP0A6T9. 2 interactions.
STRINGi511145.b2904.

Proteomic databases

EPDiP0A6T9.
PaxDbiP0A6T9.
PRIDEiP0A6T9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75942; AAC75942; b2904.
BAE76969; BAE76969; BAE76969.
GeneIDi947393.
KEGGiecj:JW2872.
eco:b2904.
PATRICi32121222. VBIEscCol129921_2999.

Organism-specific databases

EchoBASEiEB0366.
EcoGeneiEG10371. gcvH.

Phylogenomic databases

eggNOGiCOG0509. LUCA.
HOGENOMiHOG000239392.
InParanoidiP0A6T9.
KOiK02437.
OMAiNTDPYGE.
PhylomeDBiP0A6T9.

Enzyme and pathway databases

BioCyciEcoCyc:GCVH-MONOMER.
ECOL316407:JW2872-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A6T9.
PROiP0A6T9.

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_ECOLI
AccessioniPrimary (citable) accession number: P0A6T9
Secondary accession number(s): P23884, Q2M9T7, Q8Z3W9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.