Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glycine dehydrogenase (decarboxylating)

Gene

gcvP

Organism
Burkholderia cenocepacia (strain MC0-3)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

Glycine + [glycine-cleavage complex H protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N(6)-dihydrolipoyl-L-lysine + CO2.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciBCEN406425:GHD9-161-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine dehydrogenase (decarboxylating)UniRule annotation (EC:1.4.4.2UniRule annotation)
Alternative name(s):
Glycine cleavage system P-proteinUniRule annotation
Glycine decarboxylaseUniRule annotation
Glycine dehydrogenase (aminomethyl-transferring)UniRule annotation
Gene namesi
Name:gcvPUniRule annotation
Ordered Locus Names:Bcenmc03_0157
OrganismiBurkholderia cenocepacia (strain MC0-3)
Taxonomic identifieri406425 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
ProteomesiUP000002169 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 975975Glycine dehydrogenase (decarboxylating)PRO_1000190208Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei723 – 7231N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliB1JSZ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GcvP family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1003.
HOGENOMiHOG000239369.
KOiK00281.
OMAiMAGMYAV.
OrthoDBiEOG6HMXDX.

Family and domain databases

Gene3Di3.40.640.10. 2 hits.
HAMAPiMF_00711. GcvP.
InterProiIPR003437. GcvP.
IPR020580. GDC-P_N.
IPR020581. GDC_P.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11773. PTHR11773. 1 hit.
PfamiPF02347. GDC-P. 2 hits.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 3 hits.
TIGRFAMsiTIGR00461. gcvP. 1 hit.

Sequencei

Sequence statusi: Complete.

B1JSZ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLEHPDRLM NRTPLSLAAL ETHDAFAERH IGPDAASQQA MLDTLGFASR
60 70 80 90 100
AALIDAVIPA SIRRAETLPL GPFAQPKSEA EALAALRALA DKNQVFRSYI
110 120 130 140 150
GQGYHDTHTP AVILRNVLEN PAWYTAYTPY QPEISQGRLE ALLNFQQMVA
160 170 180 190 200
DLTGLAISNA SLLDEATAAA EAMTLLQRTG KPKSNVFYVA DDVLPQTLEV
210 220 230 240 250
IRTRALPIGI EVKTGPAADA AQANAFGVLL QYPGVNGDVR DYRALTDAIH
260 270 280 290 300
AAGGHVVVAA DLLALTVLTP PGEWGADVAI GNTQRFGVPM GFGGPHAAYL
310 320 330 340 350
AVRDEFKRQM PGRLVGVTVD AQGKPALRLA LQTREQHIRR EKATSNVCTA
360 370 380 390 400
QALLAIMASM YAVYHGPHGL KTIALRVNRI AALLAAGVKQ LGFATVNDTF
410 420 430 440 450
FDTLTIDTGA RTAQVHEFAK AKRINLRRVS DTQVGVSVDE TTTRDDLADL
460 470 480 490 500
LDVFAQAAGG TAPAVDALDA GLAGVAALPA GLERTSAYLT HHVFNRHHSE
510 520 530 540 550
TEMLRYLRSL SDKDLALDRS MIPLGSCTMK LNATSEMLPV TWPEFGGIHP
560 570 580 590 600
FAPAEQTVGY REMIDQLEQM LVAATGYAAV SLQPNAGSQG EYAGLLIIHA
610 620 630 640 650
YHASRGEGHR DVCLIPASAH GTNPASAHMA GMKVVVVACD AQGNVDIADL
660 670 680 690 700
KAKAEQHSAN LAAIMITYPS THGVFEQNVR EICEIVHAHG GQVYVDGANM
710 720 730 740 750
NAMVGLTAPG QFGGDVSHLN LHKTFCIPHG GGGPGVGPVA VGAHLAKFLP
760 770 780 790 800
NQRSTGYARA EDGIGAVSAA PYGSASILPI SWMYIAMMGA KNLTAATETA
810 820 830 840 850
ILNANYIAKR LAPHYPVLYS GPGGLVAHEC ILDLRPIKES SGISVDDVAK
860 870 880 890 900
RLMDYGFHAP TMSFPVPGTL MVEPTESESQ EELDRFIAAM IAIREEIRAV
910 920 930 940 950
EEGRADREDN PLRHAPHTAA VVTANEWPHA YSREQAAYPV ASLGTNKYWP
960 970
PVGRADNAYG DRNLFCSCVP MSDYA
Length:975
Mass (Da):104,150
Last modified:April 29, 2008 - v1
Checksum:i7B694E84D15E2130
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000958 Genomic DNA. Translation: ACA89337.1.
RefSeqiWP_012327634.1. NC_010508.1.

Genome annotation databases

EnsemblBacteriaiACA89337; ACA89337; Bcenmc03_0157.
KEGGibcm:Bcenmc03_0157.
PATRICi19087202. VBIBurCen61509_0157.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000958 Genomic DNA. Translation: ACA89337.1.
RefSeqiWP_012327634.1. NC_010508.1.

3D structure databases

ProteinModelPortaliB1JSZ2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACA89337; ACA89337; Bcenmc03_0157.
KEGGibcm:Bcenmc03_0157.
PATRICi19087202. VBIBurCen61509_0157.

Phylogenomic databases

eggNOGiCOG1003.
HOGENOMiHOG000239369.
KOiK00281.
OMAiMAGMYAV.
OrthoDBiEOG6HMXDX.

Enzyme and pathway databases

BioCyciBCEN406425:GHD9-161-MONOMER.

Family and domain databases

Gene3Di3.40.640.10. 2 hits.
HAMAPiMF_00711. GcvP.
InterProiIPR003437. GcvP.
IPR020580. GDC-P_N.
IPR020581. GDC_P.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERiPTHR11773. PTHR11773. 1 hit.
PfamiPF02347. GDC-P. 2 hits.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 3 hits.
TIGRFAMsiTIGR00461. gcvP. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-3."
    Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.
    , Kyrpides N., Mikhailova N., Tiedje J., Richardson P.
    Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MC0-3.

Entry informationi

Entry nameiGCSP_BURCC
AccessioniPrimary (citable) accession number: B1JSZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: July 22, 2015
This is version 59 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.