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Protein

Glycine dehydrogenase (decarboxylating)

Gene

gcvP

Organism
Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD))
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

  1. glycine dehydrogenase (decarboxylating) activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. glycine decarboxylation via glycine cleavage system Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciBAMB339670:GH48-133-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:Bamb_0131
OrganismiBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD))
Taxonomic identifieri339670 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
ProteomesiUP000000662: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 975975Glycine dehydrogenase (decarboxylating)PRO_1000045570Add
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

Protein-protein interaction databases

STRINGi339670.Bamb_0131.

Structurei

3D structure databases

ProteinModelPortaliQ0BJI1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GcvP family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1003.
HOGENOMiHOG000239369.
KOiK00281.
OMAiRAESEMT.
OrthoDBiEOG6HMXDX.

Family and domain databases

Gene3Di3.40.640.10. 2 hits.
HAMAPiMF_00711. GcvP.
InterProiIPR020580. GDC-P_N.
IPR020581. GDC_P.
IPR003437. GDC_P_homo.
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.

Q0BJI1-1 [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 KPASNVFYVA DDVLPQTLEV
210 220 230 240 250
IRTRALPVGI EVKTGPAADA AQANAFGVLL QYPGVNGDVR DYRALTEAIH
260 270 280 290 300
AAGGHVVVAA DLLALTVLTP PGEWGADVAV GNTQRFGVPM GFGGPHAAYL
310 320 330 340 350
AVRDEFKRQM PGRLVGVTVD AQGKPALRLA LQTREQHIRR EKATSNVCTA
360 370 380 390 400
QALLAIMASM YAVYHGPHGL KTIALRVNRI AALFAAGVKQ LGFAPINDTF
410 420 430 440 450
FDTLTIDTGA RTAQVHEFAK ARRINLRRVS DTQVGVSFDE TTTRDDLAAL
460 470 480 490 500
LAVFAQAAGG TAPSVDALDA GLAGVAALPA GLERTSAYLT HHVFNRHHSE
510 520 530 540 550
TEMLRYLRSL SDKDLALDRS MIPLGSCTMK LNATSEMLPV TWPEFGRIHP
560 570 580 590 600
FAPAEQTVGY REMIDQLEQM LVAATGYAAV SLQPNAGSQG EYAGLLIIHA
610 620 630 640 650
YHASRGEAHR DVCLIPASAH GTNPASAHMA GMKVVVVACD AQGNVDIADL
660 670 680 690 700
KAKAEQHAND LAAIMITYPS THGVFEQNVR EICEIVHAHG GQVYVDGANM
710 720 730 740 750
NAMVGLTAPG QFGGDVSHLN LHKTFCIPHG GGGPGVGPVA VGPHLAKFLP
760 770 780 790 800
NQRSTGYTRE ENGIGAVSAA PYGSASILPI SWMYIAMMGA KNLTAATETA
810 820 830 840 850
ILNANYIAKR LAPHYPVLYS GPGGLVAHEC ILDLRPIKET 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):104,396
Last modified:October 17, 2006 - v1
Checksum:iAABFDF60460FCDB2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000440 Genomic DNA. Translation: ABI85692.1.
RefSeqiWP_011655652.1. NC_008390.1.
YP_772026.1. NC_008390.1.

Genome annotation databases

EnsemblBacteriaiABI85692; ABI85692; Bamb_0131.
GeneIDi4309200.
KEGGibam:Bamb_0131.
PATRICi19015708. VBIBurAmb61564_0182.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000440 Genomic DNA. Translation: ABI85692.1.
RefSeqiWP_011655652.1. NC_008390.1.
YP_772026.1. NC_008390.1.

3D structure databases

ProteinModelPortaliQ0BJI1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi339670.Bamb_0131.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI85692; ABI85692; Bamb_0131.
GeneIDi4309200.
KEGGibam:Bamb_0131.
PATRICi19015708. VBIBurAmb61564_0182.

Phylogenomic databases

eggNOGiCOG1003.
HOGENOMiHOG000239369.
KOiK00281.
OMAiRAESEMT.
OrthoDBiEOG6HMXDX.

Enzyme and pathway databases

BioCyciBAMB339670:GH48-133-MONOMER.

Family and domain databases

Gene3Di3.40.640.10. 2 hits.
HAMAPiMF_00711. GcvP.
InterProiIPR020580. GDC-P_N.
IPR020581. GDC_P.
IPR003437. GDC_P_homo.
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 cepacia AMMD."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.
    , Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K., Ramette A., Tiedje J., Richardson P.
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-244 / AMMD.

Entry informationi

Entry nameiGCSP_BURCM
AccessioniPrimary (citable) accession number: Q0BJI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 2006
Last modified: February 4, 2015
This is version 67 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.