ID   GCSP2_ARATH             Reviewed;        1044 AA.
AC   O80988; Q0WV94;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=Glycine dehydrogenase (decarboxylating) 2, mitochondrial;
DE            EC=1.4.4.2;
DE   AltName: Full=Glycine cleavage system P protein 2;
DE   AltName: Full=Glycine decarboxylase 2;
DE   AltName: Full=Glycine decarboxylase P-protein 2;
DE            Short=AtGLDP2;
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) 2;
DE   Flags: Precursor;
GN   Name=GLDP2; Synonyms=GDCSP, GDP2; OrderedLocusNames=At2g26080;
GN   ORFNames=T19L18.11;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   REVIEW.
RX   PubMed=11286922; DOI=10.1016/s1360-1385(01)01892-1;
RA   Douce R., Bourguignon J., Neuburger M., Rebeille F.;
RT   "The glycine decarboxylase system: a fascinating complex.";
RL   Trends Plant Sci. 6:167-176(2001).
RN   [5]
RP   REVIEW, AND NOMENCLATURE.
RX   PubMed=12730263; DOI=10.1093/jxb/erg171;
RA   Bauwe H., Kolukisaoglu U.;
RT   "Genetic manipulation of glycine decarboxylation.";
RL   J. Exp. Bot. 54:1523-1535(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT   signaling and regulatory components, provides assessment of targeting
RT   prediction programs, and indicates plant-specific mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia, and cv. Wassilewskija;
RX   PubMed=17496108; DOI=10.1104/pp.107.099317;
RA   Engel N., van den Daele K., Kolukisaoglu U., Morgenthal K., Weckwerth W.,
RA   Paernik T., Keerberg O., Bauwe H.;
RT   "Deletion of glycine decarboxylase in Arabidopsis is lethal under
RT   nonphotorespiratory conditions.";
RL   Plant Physiol. 144:1328-1335(2007).
CC   -!- FUNCTION: The glycine decarboxylase (GDC) or glycine cleavage system
CC       catalyzes the degradation of glycine. The P protein binds the alpha-
CC       amino group of glycine through its pyridoxal phosphate cofactor; CO(2)
CC       is released and the remaining methylamine moiety is then transferred to
CC       the lipoamide cofactor of the H protein (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:17496108}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] +
CC         glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-
CC         [glycine-cleavage complex H protein] + CO2; Xref=Rhea:RHEA:24304,
CC         Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83143; EC=1.4.4.2;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer (By similarity). The glycine cleavage system is
CC       composed of four proteins: P, T, L and H. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves. Detected in roots, stems,
CC       flowers and siliques. {ECO:0000269|PubMed:17496108}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy with
CC       GLDP1. Gldp1 and gldp2 double mutants have a seedling development
CC       arrested at the cotyledon stage even under nonphotorespiratory
CC       conditions. {ECO:0000269|PubMed:17496108}.
CC   -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000305}.
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DR   EMBL; AC004747; AAC31228.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07793.1; -; Genomic_DNA.
DR   EMBL; AK226865; BAE98954.1; -; mRNA.
DR   PIR; T02615; T02615.
DR   RefSeq; NP_180178.1; NM_128167.4.
DR   AlphaFoldDB; O80988; -.
DR   SMR; O80988; -.
DR   BioGRID; 2501; 7.
DR   STRING; 3702.AT2G26080.1; -.
DR   iPTMnet; O80988; -.
DR   MetOSite; O80988; -.
DR   SwissPalm; O80988; -.
DR   PaxDb; O80988; -.
DR   PRIDE; O80988; -.
DR   ProteomicsDB; 221960; -.
DR   EnsemblPlants; AT2G26080.1; AT2G26080.1; AT2G26080.
DR   GeneID; 817149; -.
DR   Gramene; AT2G26080.1; AT2G26080.1; AT2G26080.
DR   KEGG; ath:AT2G26080; -.
DR   Araport; AT2G26080; -.
DR   TAIR; locus:2057464; AT2G26080.
DR   eggNOG; KOG2040; Eukaryota.
DR   HOGENOM; CLU_004620_1_1_1; -.
DR   InParanoid; O80988; -.
DR   OMA; DEHCHPQ; -.
DR   OrthoDB; 390348at2759; -.
DR   PhylomeDB; O80988; -.
DR   BioCyc; ARA:AT2G26080-MON; -.
DR   PRO; PR:O80988; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O80988; baseline and differential.
DR   Genevisible; O80988; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0005773; C:vacuole; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR   GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR   CDD; cd00613; GDC-P; 2.
DR   Gene3D; 3.40.640.10; -; 2.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR003437; GcvP.
DR   InterPro; IPR020581; GDC_P.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11773; PTHR11773; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; SSF53383; 2.
DR   TIGRFAMs; TIGR00461; gcvP; 1.
PE   1: Evidence at protein level;
KW   Mitochondrion; Oxidoreductase; Pyridoxal phosphate; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..72
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000305"
FT   CHAIN           73..1044
FT                   /note="Glycine dehydrogenase (decarboxylating) 2,
FT                   mitochondrial"
FT                   /id="PRO_0000010743"
FT   MOD_RES         780
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        534
FT                   /note="A -> T (in Ref. 3; BAE98954)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1044 AA;  113776 MW;  227C30B67D82A97D CRC64;
     MERARRLAYR GIVKRLVNET KRHRNGESSL LPTTTVTPSR YVSSVSSFLH RRRDVSGSAF
     TTSGRNQHQT RSISVDALKP SDTFPRRHNS ATPDEQAQMA NYCGFDNLNT LIDSTVPKSI
     RLDSMKFSGI FDEGLTESQM IEHMSDLASK NKVFKSFIGM GYYNTHVPPV ILRNIMENPA
     WYTQYTPYQA EISQGRLESL LNYQTVITDL TGLPMSNASL LDEGTAAAEA MAMCNNILKG
     KKKTFVIASN CHPQTIDVCK TRADGFDLKV VTVDIKDVDY SSGDVCGVLV QYPGTEGEVL
     DYGEFVKNAH ANGVKVVMAT DLLALTMLKP PGEFGADIVV GSGQRFGVPM GYGGPHAAFL
     ATSQEYKRMM PGRIIGVSVD SSGKQALRMA MQTREQHIRR DKATSNICTA QALLANMTAM
     YAVYHGPEGL KSIAQRVHGL AGVFALGLKK LGTAQVQDLP FFDTVKVTCS DATAIFDVAA
     KKEINLRLVD SNTITVAFDE TTTLDDVDKL FEVFASGKPV QFTAESLAPE FNNAIPSSLT
     RESPYLTHPI FNMYHTEHEL LRYIHKLQNK DLSLCHSMIP LGSCTMKLNA TTEMMPVTWP
     SFTNMHPFAP VEQAQGYQEM FTNLGELLCT ITGFDSFSLQ PNAGAAGEYA GLMVIRAYHM
     SRGDHHRNVC IIPVSAHGTN PASAAMCGMK IVAVGTDAKG NINIEELRNA AEANKDNLAA
     LMVTYPSTHG VYEEGIDEIC NIIHENGGQV YMDGANMNAQ VGLTSPGFIG ADVCHLNLHK
     TFCIPHGGGG PGMGPIGVKQ HLAPFLPSHP VIPTGGIPEP EQTSPLGTIS AAPWGSALIL
     PISYTYIAMM GSGGLTDASK IAILNANYMA KRLESHYPVL FRGVNGTVAH EFIIDLRGFK
     NTAGIEPEDV AKRLMDYGFH GPTMSWPVPG TLMIEPTESE SKAELDRFCD ALISIREEIS
     QIEKGNADPN NNVLKGAPHP PSLLMADTWK KPYSREYAAF PAPWLRSSKF WPTTGRVDNV
     YGDRNLVCTL QPANEEQAAA AVSA