Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q94B78 (GCSP1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycine dehydrogenase (decarboxylating) 1, mitochondrial

EC=1.4.4.2
Alternative name(s):
Glycine cleavage system P protein 1
Glycine decarboxylase 1
Glycine decarboxylase P-protein 1
Short name=AtGLDP1
Glycine dehydrogenase (aminomethyl-transferring) 1
Gene names
Name:GLDP1
Synonyms:GDP1
Ordered Locus Names:At4g33010
ORF Names:F26P21.130
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1037 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The glycine decarboxylase (GDC) or 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 By similarity. Ref.7

Catalytic activity

Glycine + [glycine-cleavage complex H protein]-N(6)-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N(6)-dihydrolipoyl-L-lysine + CO2. HAMAP-Rule MF_00711

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_00711

Enzyme regulation

Inhibited by harpin, S-nitrosoglutathione (GSNO), nitric oxide, N-ethylmaleimide and 5,5'-dithiobis-(2-nitrobenzoic acid). Ref.8

Subunit structure

Homodimer By similarity. The glycine cleavage system is composed of four proteins: P, T, L and H. HAMAP-Rule MF_00711

Subcellular location

Mitochondrion Ref.6.

Tissue specificity

Expressed in leaves. Detected in roots, stems, flowers and siliques. Ref.7

Post-translational modification

Glutathionylated at Cys-98, Cys-777, Cys-943 and Cys-1022 after S-nitrosoglutathione treatment. HAMAP-Rule MF_00711

S-nitrosylated at unknown positions by nitric oxide. HAMAP-Rule MF_00711

Disruption phenotype

No visible phenotype; due to the redundancy with GLDP2. Gldp1 and gldp2 double mutants have a seedling development arrested at the cotyledon stage even under nonphotorespiratory conditions. Ref.7

Sequence similarities

Belongs to the GcvP family.

Caution

This protein has also been shown to act as an inducible nitric oxide synthase (iNOS) (PubMed:12757708), but the paper has been retracted (PubMed:15599984).

Sequence caution

The sequence AAN17423.1 differs from that shown. Reason: Frameshift at position 942.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q94B78-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3939Mitochondrion Potential
Chain40 – 1037998Glycine dehydrogenase (decarboxylating) 1, mitochondrial HAMAP-Rule MF_00711
PRO_0000010744

Amino acid modifications

Modified residue981S-glutathionyl cysteine; transient HAMAP-Rule MF_00711
Modified residue4021S-glutathionyl cysteine HAMAP-Rule MF_00711
Modified residue4631S-glutathionyl cysteine HAMAP-Rule MF_00711
Modified residue7741N6-(pyridoxal phosphate)lysine By similarity
Modified residue7771S-glutathionyl cysteine; transient HAMAP-Rule MF_00711
Modified residue9431S-glutathionyl cysteine; transient HAMAP-Rule MF_00711
Modified residue10221S-glutathionyl cysteine; transient HAMAP-Rule MF_00711

Experimental info

Sequence conflict5781C → R in AAN17423. Ref.3
Sequence conflict8841H → R in AAL57651. Ref.3
Sequence conflict8841H → R in AAN64523. Ref.3
Sequence conflict9251T → A in AAN17423. Ref.3
Sequence conflict10321A → T in AAK68740. Ref.3
Sequence conflict10321A → T in AAM91322. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 26, 2004. Version 2.
Checksum: 168C11DB642687A5

FASTA1,037112,925
        10         20         30         40         50         60 
MERARRLAYR GIVKRLVNDT KRHRNAETPH LVPHAPARYV SSLSPFISTP RSVNHTAAFG 

        70         80         90        100        110        120 
RHQQTRSISV DAVKPSDTFP RRHNSATPDE QTHMAKFCGF DHIDSLIDAT VPKSIRLDSM 

       130        140        150        160        170        180 
KFSKFDAGLT ESQMIQHMVD LASKNKVFKS FIGMGYYNTH VPTVILRNIM ENPAWYTQYT 

       190        200        210        220        230        240 
PYQAEISQGR LESLLNFQTV ITDLTGLPMS NASLLDEGTA AAEAMAMCNN ILKGKKKTFV 

       250        260        270        280        290        300 
IASNCHPQTI DVCKTRADGF DLKVVTSDLK DIDYSSGDVC GVLVQYPGTE GEVLDYAEFV 

       310        320        330        340        350        360 
KNAHANGVKV VMATDLLALT VLKPPGEFGA DIVVGSAQRF GVPMGYGGPH AAFLATSQEY 

       370        380        390        400        410        420 
KRMMPGRIIG ISVDSSGKQA LRMAMQTREQ HIRRDKATSN ICTAQALLAN MAAMYAVYHG 

       430        440        450        460        470        480 
PAGLKSIAQR VHGLAGIFSL GLNKLGVAEV QELPFFDTVK IKCSDAHAIA DAASKSEINL 

       490        500        510        520        530        540 
RVVDSTTITA SFDETTTLDD VDKLFKVFAS GKPVPFTAES LAPEVQNSIP SSLTRESPYL 

       550        560        570        580        590        600 
THPIFNMYHT EHELLRYIHK LQSKDLSLCH SMIPLGSCTM KLNATTEMMP VTWPSFTDIH 

       610        620        630        640        650        660 
PFAPVEQAQG YQEMFENLGD LLCTITGFDS FSLQPNAGAA GEYAGLMVIR AYHMSRGDHH 

       670        680        690        700        710        720 
RNVCIIPVSA HGTNPASAAM CGMKIITVGT DAKGNINIEE VRKAAEANKD NLAALMVTYP 

       730        740        750        760        770        780 
STHGVYEEGI DEICNIIHEN GGQVYMDGAN MNAQVGLTSP GFIGADVCHL NLHKTFCIPH 

       790        800        810        820        830        840 
GGGGPGMGPI GVKNHLAPFL PSHPVIPTGG IPQPEKTAPL GAISAAPWGS ALILPISYTY 

       850        860        870        880        890        900 
IAMMGSGGLT DASKIAILNA NYMAKRLEKH YPVLFRGVNG TVAHEFIIDL RGFKNTAGIE 

       910        920        930        940        950        960 
PEDVAKRLMD YGFHGPTMSW PVPGTLMIEP TESESKAELD RFCDALISIR EEIAQIEKGN 

       970        980        990       1000       1010       1020 
ADVQNNVLKG APHPPSLLMA DTWKKPYSRE YAAFPAPWLR SSKFWPTTGR VDNVYGDRKL 

      1030 
VCTLLPEEEQ VAAAVSA 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"The glycine decarboxylase system: a fascinating complex."
Douce R., Bourguignon J., Neuburger M., Rebeille F.
Trends Plant Sci. 6:167-176(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[5]"Genetic manipulation of glycine decarboxylation."
Bauwe H., Kolukisaoglu U.
J. Exp. Bot. 54:1523-1535(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, NOMENCLATURE.
[6]"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: cv. Landsberg erecta.
[7]"Deletion of glycine decarboxylase in Arabidopsis is lethal under nonphotorespiratory conditions."
Engel N., van den Daele K., Kolukisaoglu U., Morgenthal K., Weckwerth W., Paernik T., Keerberg O., Bauwe H.
Plant Physiol. 144:1328-1335(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
Strain: cv. Columbia and cv. Wassilewskija.
[8]"Regulation of plant glycine decarboxylase by s-nitrosylation and glutathionylation."
Palmieri M.C., Lindermayr C., Bauwe H., Steinhauser C., Durner J.
Plant Physiol. 152:1514-1528(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, S-NITROSYLATION, GLUTATHIONYLATION AT CYS-98; CYS-402; CYS-463; CYS-777; CYS-943 AND CYS-1022.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL031804 Genomic DNA. Translation: CAA21210.1.
AL161582 Genomic DNA. Translation: CAB80018.1.
CP002687 Genomic DNA. Translation: AEE86159.1.
AY063903 mRNA. Translation: AAL36259.1.
AY091186 mRNA. Translation: AAM14125.1.
AY042800 mRNA. Translation: AAK68740.1.
AY128922 mRNA. Translation: AAM91322.1.
AY065004 mRNA. Translation: AAL57651.1.
BT001132 mRNA. Translation: AAN64523.1.
BT000446 mRNA. Translation: AAN17423.1. Frameshift.
PIRT05309.
RefSeqNP_195027.1. NM_119455.2.
UniGeneAt.22214.
At.24550.

3D structure databases

ProteinModelPortalQ94B78.
SMRQ94B78. Positions 67-1023.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid14723. 1 interaction.
IntActQ94B78. 1 interaction.
MINTMINT-8070384.

Proteomic databases

PRIDEQ94B78.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G33010.1; AT4G33010.1; AT4G33010. [Q94B78-1]
GeneID829438.
KEGGath:AT4G33010.

Organism-specific databases

GeneFarm1737. 130.
TAIRAT4G33010.

Phylogenomic databases

HOGENOMHOG000239369.
InParanoidQ94B78.
KOK00281.
OMAHTQVDLM.
PhylomeDBQ94B78.
ProtClustDBPLN02414.

Enzyme and pathway databases

BioCycARA:AT4G33010-MONOMER.
ARA:GQT-949-MONOMER.

Gene expression databases

ArrayExpressQ94B78.
GenevestigatorQ94B78.

Family and domain databases

Gene3D3.40.640.10. 2 hits.
HAMAPMF_00711. GcvP.
InterProIPR020580. GDC-P_N.
IPR020581. GDC_P.
IPR003437. GDC_P_homo.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERPTHR11773. PTHR11773. 1 hit.
PfamPF02347. GDC-P. 2 hits.
[Graphical view]
SUPFAMSSF53383. SSF53383. 3 hits.
TIGRFAMsTIGR00461. gcvP. 1 hit.
ProtoNetSearch...

Other

PROQ94B78.

Entry information

Entry nameGCSP1_ARATH
AccessionPrimary (citable) accession number: Q94B78
Secondary accession number(s): O82642, Q8GTY1, Q8VZF0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: April 16, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names