O80988 (GCSP2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycine dehydrogenase [decarboxylating] 2, mitochondrial
EC=1.4.4.2

Alternative name(s):
Glycine cleavage system P protein 2
Glycine decarboxylase 2
Glycine decarboxylase P-protein 2
Short name=AtGLDP2

Gene names

Name:	GLDP2
Synonyms:	GDCSP, GDP2
Ordered Locus Names:	At2g26080
ORF Names:	T19L18.11

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	1044 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Catalytic activity	Glycine + H-protein-lipoyllysine = H-protein-S-aminomethyldihydrolipoyllysine + CO2.
Cofactor	Pyridoxal phosphate By similarity.
Subunit structure	Homodimer By similarity. The glycine cleavage system is composed of four proteins: P, T, L and H.
Subcellular location	Mitochondrion.
Tissue specificity	Expressed in leaves. Detected in roots, stems, flowers and siliques.
Disruption phenotype	No visible phenotype, due to the redundancy with GLDP1. Double mutants gldp1/gldp2 have a seedling development arrested at the cotyledon stage even under nonphotorespiratory conditions.
Sequence similarities	Belongs to the GcvP family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyridoxal phosphate
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycine catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	apoplast Inferred from direct assay PubMed 21798377. Source: TAIR chloroplast envelope Inferred from direct assay PubMed 12938931. Source: TAIR mitochondrion Inferred from direct assay Ref.6PubMed 17137349PubMed 18385124. Source: TAIR
Molecular_function	ATP binding Inferred from direct assay PubMed 17137349. Source: TAIR glycine dehydrogenase (decarboxylating) activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 72	72	Mitochondrion Potential
	Chain	73 – 1044	972	Glycine dehydrogenase [decarboxylating] 2, mitochondrial		PRO_0000010743
Amino acid modifications
	Modified residue	780	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Sequence conflict	534	1	A → T in BAE98954. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O80988 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 227C30B67D82A97D	FASTA	1,044	113,776
	10 20 30 40 50 60 MERARRLAYR GIVKRLVNET KRHRNGESSL LPTTTVTPSR YVSSVSSFLH RRRDVSGSAF 70 80 90 100 110 120 TTSGRNQHQT RSISVDALKP SDTFPRRHNS ATPDEQAQMA NYCGFDNLNT LIDSTVPKSI 130 140 150 160 170 180 RLDSMKFSGI FDEGLTESQM IEHMSDLASK NKVFKSFIGM GYYNTHVPPV ILRNIMENPA 190 200 210 220 230 240 WYTQYTPYQA EISQGRLESL LNYQTVITDL TGLPMSNASL LDEGTAAAEA MAMCNNILKG 250 260 270 280 290 300 KKKTFVIASN CHPQTIDVCK TRADGFDLKV VTVDIKDVDY SSGDVCGVLV QYPGTEGEVL 310 320 330 340 350 360 DYGEFVKNAH ANGVKVVMAT DLLALTMLKP PGEFGADIVV GSGQRFGVPM GYGGPHAAFL 370 380 390 400 410 420 ATSQEYKRMM PGRIIGVSVD SSGKQALRMA MQTREQHIRR DKATSNICTA QALLANMTAM 430 440 450 460 470 480 YAVYHGPEGL KSIAQRVHGL AGVFALGLKK LGTAQVQDLP FFDTVKVTCS DATAIFDVAA 490 500 510 520 530 540 KKEINLRLVD SNTITVAFDE TTTLDDVDKL FEVFASGKPV QFTAESLAPE FNNAIPSSLT 550 560 570 580 590 600 RESPYLTHPI FNMYHTEHEL LRYIHKLQNK DLSLCHSMIP LGSCTMKLNA TTEMMPVTWP 610 620 630 640 650 660 SFTNMHPFAP VEQAQGYQEM FTNLGELLCT ITGFDSFSLQ PNAGAAGEYA GLMVIRAYHM 670 680 690 700 710 720 SRGDHHRNVC IIPVSAHGTN PASAAMCGMK IVAVGTDAKG NINIEELRNA AEANKDNLAA 730 740 750 760 770 780 LMVTYPSTHG VYEEGIDEIC NIIHENGGQV YMDGANMNAQ VGLTSPGFIG ADVCHLNLHK 790 800 810 820 830 840 TFCIPHGGGG PGMGPIGVKQ HLAPFLPSHP VIPTGGIPEP EQTSPLGTIS AAPWGSALIL 850 860 870 880 890 900 PISYTYIAMM GSGGLTDASK IAILNANYMA KRLESHYPVL FRGVNGTVAH EFIIDLRGFK 910 920 930 940 950 960 NTAGIEPEDV AKRLMDYGFH GPTMSWPVPG TLMIEPTESE SKAELDRFCD ALISIREEIS 970 980 990 1000 1010 1020 QIEKGNADPN NNVLKGAPHP PSLLMADTWK KPYSREYAAF PAPWLRSSKF WPTTGRVDNV 1030 1040 YGDRNLVCTL QPANEEQAAA AVSA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(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]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC004747 Genomic DNA. Translation: AAC31228.1. CP002685 Genomic DNA. Translation: AEC07793.1. AK226865 mRNA. Translation: BAE98954.1.
IPI	IPI00526682.
PIR	T02615.
RefSeq	NP_180178.1. NM_128167.3.
UniGene	At.24550. At.72082.
3D structure databases
ProteinModelPortal	O80988.
SMR	O80988. Positions 92-463, 529-952.
ModBase	Search...
Proteomic databases
PaxDb	O80988.
PRIDE	O80988.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G26080.1; AT2G26080.1; AT2G26080.
GeneID	817149.
KEGG	ath:AT2G26080.
Organism-specific databases
GeneFarm	1741. 130.
TAIR	At2g26080.
Phylogenomic databases
eggNOG	COG1003.
HOGENOM	HOG000239369.
InParanoid	O80988.
KO	K00281.
OMA	PVSRIDN.
PhylomeDB	O80988.
ProtClustDB	PLN02414.
Gene expression databases
ArrayExpress	O80988.
Genevestigator	O80988.
GermOnline	AT2G26080. Arabidopsis thaliana.
Family and domain databases
Gene3D	3.40.640.10. 2 hits.
HAMAP	MF_00711. GcvP.
InterPro	IPR020580. GDC-P_N. IPR020581. GDC_P. IPR003437. GDC_P_homo. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
PANTHER	PTHR11773. PTHR11773. 1 hit.
Pfam	PF02347. GDC-P. 2 hits. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 2 hits.
TIGRFAMs	TIGR00461. gcvP. 1 hit.
ProtoNet	Search...

Entry information

Entry name

GCSP2_ARATH

Accession

Primary (citable) accession number: O80988
Secondary accession number(s): Q0WV94

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program