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Protein

Glycine dehydrogenase (decarboxylating)

Gene

gcvP

Organism
Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019)
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

BioCyciMBOV561275:GHDN-1873-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:JTY_1851
OrganismiMycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019)
Taxonomic identifieri561275 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000002205 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 941941Glycine dehydrogenase (decarboxylating)PRO_1000147966Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei692 – 6921N6-(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

STRINGi561275.JTY_1851.

Structurei

3D structure databases

ProteinModelPortaliC1APA9.
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.

C1APA9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDHSTFADR HIGLDSQAVA TMLAVIGVDS LDDLAVKAVP AGILDTLTDT
60 70 80 90 100
GAAPGLDSLP PAASEAEALA ELRALADANT VAVSMIGQGY YDTHTPPVLL
110 120 130 140 150
RNIIENPAWY TAYTPYQPEI SQGRLEALLN FQTLVTDLTG LEIANASMLD
160 170 180 190 200
EGTAAAEAMT LMHRAARGPV KRVVVDADVF TQTAAVLATR AKPLGIEIVT
210 220 230 240 250
ADLRAGLPDG EFFGAIAQLP GASGRITDWS ALVQQAHDRG ALVAVGADLL
260 270 280 290 300
ALTLIAPPGE IGADVAFGTT QRFGVPMGFG GPHAGYLAVH AKHARQLPGR
310 320 330 340 350
LVGVSVDSDG TPAYRLALQT REQHIRRDKA TSNICTAQVL LAVLAAMYAS
360 370 380 390 400
YHGAGGLTAI ARRVHAHAEA IAGALGDALV HDKYFDTVLA RVPGRADEVL
410 420 430 440 450
ARAKANGINL WRVDADHVSV ACDEATTDTH VAVVLDAFGV AAAAPAHADI
460 470 480 490 500
ATRTSEFLTH PAFTQYRTET SMMRYLRALA DKDIALDRSM IPLGSCTMKL
510 520 530 540 550
NAAAEMESIT WPEFGRQHPF APASDTAGLR QLVADLQSWL VLITGYDAVS
560 570 580 590 600
LQPNAGSQGE YAGLLAIHEY HASRGEPHRD ICLIPSSAHG TNAASAALAG
610 620 630 640 650
MRVVVVDCHD NGDVDLDDLR AKVGEHAERL SALMITYPST HGVYEHDIAE
660 670 680 690 700
ICAAVHDAGG QVYVDGANLN ALVGLARPGK FGGDVSHLNL HKTFCIPHGG
710 720 730 740 750
GGPGVGPVAV RAHLAPFLPG HPFAPELPKG YPVSSAPYGS ASILPITWAY
760 770 780 790 800
IRMMGAEGLR AASLTAITSA NYIARRLDEY YPVLYTGENG MVAHECILDL
810 820 830 840 850
RGITKLTGIT VDDVAKRLAD YGFHAPTMSF PVAGTLMVEP TESESLAEVD
860 870 880 890 900
AFCEAMIGIR AEIDKVGAGE WPVDDNPLRG APHTAQCLLA SDWDHPYTRE
910 920 930 940
QAAYPLGTAF RPKVWPAVRR IDGAYGDRNL VCSCPPVEAF A
Length:941
Mass (Da):99,453
Last modified:May 25, 2009 - v1
Checksum:i4572D7C6FC2CEA8B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010918 Genomic DNA. Translation: BAH26138.1.
RefSeqiYP_002644906.1. NC_012207.1.

Genome annotation databases

EnsemblBacteriaiBAH26138; BAH26138; JTY_1851.
KEGGimbt:JTY_1851.
PATRICi18023289. VBIMycBov85238_2022.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010918 Genomic DNA. Translation: BAH26138.1.
RefSeqiYP_002644906.1. NC_012207.1.

3D structure databases

ProteinModelPortaliC1APA9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi561275.JTY_1851.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAH26138; BAH26138; JTY_1851.
KEGGimbt:JTY_1851.
PATRICi18023289. VBIMycBov85238_2022.

Phylogenomic databases

eggNOGiCOG1003.
HOGENOMiHOG000239369.
KOiK00281.
OMAiRAESEMT.
OrthoDBiEOG6HMXDX.

Enzyme and pathway databases

BioCyciMBOV561275:GHDN-1873-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. "Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains."
    Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.
    Vaccine 27:1710-1716(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BCG / Tokyo 172 / ATCC 35737 / TMC 1019.

Entry informationi

Entry nameiGCSP_MYCBT
AccessioniPrimary (citable) accession number: C1APA9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 27, 2009
Last sequence update: May 25, 2009
Last modified: March 31, 2015
This is version 42 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.