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Protein

Glycine dehydrogenase (decarboxylating)

Gene

gcvP

Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
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

BioCyciBJAP224911:GJEJ-5800-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:blr5753
OrganismiBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Taxonomic identifieri224911 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
ProteomesiUP000002526: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 955955Glycine dehydrogenase (decarboxylating)PRO_0000166907Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei702 – 7021N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PRIDEiQ89I86.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi224911.blr5753.

Structurei

3D structure databases

ProteinModelPortaliQ89I86.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GcvP family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1003.
HOGENOMiHOG000239369.
InParanoidiQ89I86.
KOiK00281.
OrthoDBiEOG6HMXDX.
PhylomeDBiQ89I86.

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.

Q89I86-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMTAHRKSNG DTTNFARRHI GPSARDVAAM LETVGAKSVD ALMAETLPAS
60 70 80 90 100
IRQAAPLDLG KPLSETEAIA HMGELAAQNQ VFTSLIGQGY SGTILPAVIQ
110 120 130 140 150
RNILENPAWY TAYTPYQPEI SQGRLEALFN FQTMICDLTG LDVANASLLD
160 170 180 190 200
EATAAAEAMA LAERHSRVEA KAFFVDKDVH PQTLAVMRTR AEPLGWNLIV
210 220 230 240 250
GDPLTDLDKA DVLGALLQYP GSSGALRDLR PAIAALKAKG ALAIVAADLL
260 270 280 290 300
ALTLLASPGE LGADIAIGSA QRFGVPMGYG GPHAAYMAVR DALKRSLPGR
310 320 330 340 350
IVGLSVDSRG MPAYRLALQT REQHIRREKA TSNICTAQVL LAVIAAMYAV
360 370 380 390 400
YHGPEGLSQI ARQVHRRAAV LAAGLRKLGF APHSDSFFDT LSVDAGAKRA
410 420 430 440 450
EIVARAAAEK INLGVGETAL RIALDETTTP ATVEAVWRAF GGQLAYAELD
460 470 480 490 500
ATTREALPEA LKRTTAFLTH PVFHAHRSET EMLRYMRKLS DRDLALDRAM
510 520 530 540 550
IPLGSCTMKL NATTEMMPLT WPEFGSLHPF APREQAKGYH ALFARLEKWL
560 570 580 590 600
CDITGYDAIS LQPNSGAQGE YAGLLAIRGY HAARGEAHRK ICLIPSSAHG
610 620 630 640 650
TNPASAAMVG MDVVVVACEK NGDVDVNDLR AKADKHANDL AAIMITYPST
660 670 680 690 700
HGVFEEHIRE ICDIVHGHGG QVYLDGANLN AQVGLSRPGD YGADVSHLNL
710 720 730 740 750
HKTFCIPHGG GGPGMGPIGV KAHLAPFLPG HPATRGDAPV GPVSAAPFGS
760 770 780 790 800
ASILTISYIY ILMMGGEGLK RATEIAILNA NYIAARLDAH FPVLYKNARG
810 820 830 840 850
RVAHECIVDP RALKTTSGVT VDDIAKRLID YGFHAPTMSF PVPGTLMIEP
860 870 880 890 900
TESESKAELD RFCDAMIAIR KEIGEVEAGR FKIEASPLRH APHTVHDIAD
910 920 930 940 950
DAWARAYSRA EGCFPDGVSR TDKYWSPVGR VDNVYGDRNL VCSCPPVSDY

AEAAE
Length:955
Mass (Da):102,392
Last modified:June 1, 2003 - v1
Checksum:i63DF72162F811292
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000040 Genomic DNA. Translation: BAC51018.1.
RefSeqiNP_772393.1. NC_004463.1.

Genome annotation databases

EnsemblBacteriaiBAC51018; BAC51018; BAC51018.
GeneIDi1049974.
KEGGibja:blr5753.
PATRICi21195266. VBIBraJap65052_5868.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000040 Genomic DNA. Translation: BAC51018.1.
RefSeqiNP_772393.1. NC_004463.1.

3D structure databases

ProteinModelPortaliQ89I86.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224911.blr5753.

Proteomic databases

PRIDEiQ89I86.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC51018; BAC51018; BAC51018.
GeneIDi1049974.
KEGGibja:blr5753.
PATRICi21195266. VBIBraJap65052_5868.

Phylogenomic databases

eggNOGiCOG1003.
HOGENOMiHOG000239369.
InParanoidiQ89I86.
KOiK00281.
OrthoDBiEOG6HMXDX.
PhylomeDBiQ89I86.

Enzyme and pathway databases

BioCyciBJAP224911:GJEJ-5800-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

Entry informationi

Entry nameiGCSP_BRADU
AccessioniPrimary (citable) accession number: Q89I86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: June 1, 2003
Last modified: January 7, 2015
This is version 74 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, Reference 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.