GCSP_PEA
ID GCSP_PEA Reviewed; 1057 AA.
AC P26969;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Glycine dehydrogenase (decarboxylating), mitochondrial;
DE EC=1.4.4.2;
DE AltName: Full=Glycine cleavage system P protein;
DE AltName: Full=Glycine decarboxylase;
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring);
DE Flags: Precursor;
GN Name=GDCSP; Synonyms=GDCP;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 87-94, TISSUE SPECIFICITY,
RP AND INDUCTION.
RC STRAIN=cv. Birte; TISSUE=Leaf;
RX PubMed=1347530; DOI=10.1016/s0021-9258(18)42773-1;
RA Turner S.R., Irland R., Rawsthorne S.;
RT "Cloning and characterization of the P subunit of glycine decarboxylase
RT from pea (Pisum sativum).";
RL J. Biol. Chem. 267:5355-5360(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 905-1057.
RC STRAIN=cv. Alaska;
RA Shah K.S., Kim Y., Oliver D.J.;
RL Submitted (AUG-1990) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. The P protein binds the alpha-amino group of glycine through
CC its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC methylamine moiety is then transferred to the lipoamide cofactor of the
CC H protein.
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 -!- SUBUNIT: Homodimer. The glycine cleavage system is composed of four
CC proteins: P, T, L and H.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves. Detected in roots and
CC embryos. {ECO:0000269|PubMed:1347530}.
CC -!- INDUCTION: Induced more than 4-fold after exposure to light for 6
CC hours. {ECO:0000269|PubMed:1347530}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000305}.
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DR EMBL; X59773; CAA42443.1; -; mRNA.
DR EMBL; X54377; CAA38252.1; -; mRNA.
DR PIR; A42109; A42109.
DR AlphaFoldDB; P26969; -.
DR SMR; P26969; -.
DR IntAct; P26969; 1.
DR PRIDE; P26969; -.
DR BRENDA; 1.4.1.27; 4872.
DR SABIO-RK; P26969; -.
DR GO; GO:0005960; C:glycine cleavage complex; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
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 Direct protein sequencing; Mitochondrion; Oxidoreductase;
KW Pyridoxal phosphate; Transit peptide.
FT TRANSIT 1..86
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1347530"
FT CHAIN 87..1057
FT /note="Glycine dehydrogenase (decarboxylating),
FT mitochondrial"
FT /id="PRO_0000010749"
FT REGION 18..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 792
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 906
FT /note="I -> Y (in Ref. 2; CAA38252)"
FT /evidence="ECO:0000305"
FT CONFLICT 919
FT /note="P -> A (in Ref. 2; CAA38252)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1057 AA; 114686 MW; 2F2EA58E9A2AC447 CRC64;
MERARRLANR ATLKRLLSEA KQNRKTESTS TTTTTPLPFS LSGSSSRYVS SVSNSILRGR
GSKPDNNVSR RVGGFLGVGY PSQSRSISVE ALKPSDTFPR RHNSATPDEQ TKMAESVGFD
TLDSLVDATV PKSIRLKEMK FNKFDGGLTE GQMIEHMKDL ASKNKVFKSF IGMGYYNTHV
PPVILRNIME NPAWYTQYTP YQAEISQGRL ESLLNFQTMI TDLTGLPMSN ASLLDEGTAA
AEAMSMCNNI QKGKKKTFII ASNCHPQTID ICQTRADGFE LKVVVKDLKD IDYKSGDVCG
VLVQYPGTEG EVLDYGEFIK KAHANEVKVV MASDLLALTV LKPPGEFGAD IVVGSAQRFG
VPMGYGGPHA AFLATSQEYK RMMPGRIIGV SVDSSGKQAL RMAMQTREQH IRRDKATSNI
CTAQALLANM AAMYAVYHGP EGLKAIAQRV HGLAGVFALG LKKLGLEVQD LGFFDTVKVK
TSNAKAIADA AIKSEINLRV VDGNTITAAF DETTTLEDVD KLFKVFAGGK PVSFTAASLA
PEFQNAIPSG LVRESPYLTH PIFNTYQTEH ELLRYIHRLQ SKDLSLCHSM IPLGSCTMKL
NATTEMMPVT WPSFTDLHPF APTEQAQGYQ EMFNNLGDLL CTITGFDSFS LQPNAGAAGE
YAGLMVIRAY HLSRGDHHRN VCIIPASAHG TNPASAAMVG MKIVTIGTDA KGNINIEELK
KAAEKHKDNL SAFMVTYPST HGVYEEGIDD ICKIIHDNGG QVYMDGANMN AQVGLTSPGW
IGADVCHLNL HKTFCIPHGG GGPGMGPIGV KKHLAPFLPS HPVVPTGGIP APENPQPLGS
ISAAPWGSAL ILPISYTYIA MMGSQGLTDA SKIAILNANY MAKRLESYYP VLFRGVNGTV
AHEFIIDLRG FKNTAGIEPE DVAKRLMDYG FHGPTMSWPV AGTLMIEPTE SESKAELDRF
CDALISIRKE IAEVEKGNAD VHNNVLKGAP HPPSLLMADA WTKPYSREYA AFPAAWLRGA
KFWPTTGRVD NVYGDRNLVC TLLPASQAVE EQAAATA
