ID GCSPB_THEKO Reviewed; 502 AA.
AC Q5JGX6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE AltName: Full=Glycine cleavage system P-protein subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE AltName: Full=Glycine decarboxylase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
GN Name=gcvPB {ECO:0000255|HAMAP-Rule:MF_00713}; OrderedLocusNames=TK1379;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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. {ECO:0000255|HAMAP-Rule:MF_00713}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC L-lysyl-[glycine-cleavage complex H protein]; 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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00713};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00713};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. In this organism, the P 'protein' is a heterodimer of two
CC subunits. {ECO:0000255|HAMAP-Rule:MF_00713}.
CC -!- SIMILARITY: Belongs to the GcvP family. C-terminal subunit subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00713}.
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DR EMBL; AP006878; BAD85568.1; -; Genomic_DNA.
DR RefSeq; WP_011250330.1; NC_006624.1.
DR AlphaFoldDB; Q5JGX6; -.
DR SMR; Q5JGX6; -.
DR IntAct; Q5JGX6; 1.
DR MINT; Q5JGX6; -.
DR STRING; 69014.TK1379; -.
DR EnsemblBacteria; BAD85568; BAD85568; TK1379.
DR GeneID; 78447899; -.
DR KEGG; tko:TK1379; -.
DR PATRIC; fig|69014.16.peg.1341; -.
DR eggNOG; arCOG00076; Archaea.
DR HOGENOM; CLU_004620_5_0_2; -.
DR InParanoid; Q5JGX6; -.
DR OrthoDB; 371967at2157; -.
DR PhylomeDB; Q5JGX6; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
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: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; 1.
DR Gene3D; 6.20.440.10; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00713; GcvPB; 1.
DR InterPro; IPR023012; GcvPB.
DR InterPro; IPR049316; GDC-P_C.
DR InterPro; IPR049315; GDC-P_N.
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:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR Pfam; PF21478; GcvP2_C; 1.
DR Pfam; PF02347; GDC-P; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Oxidoreductase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..502
FT /note="Probable glycine dehydrogenase (decarboxylating)
FT subunit 2"
FT /id="PRO_0000167030"
FT MOD_RES 273
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00713"
SQ SEQUENCE 502 AA; 55991 MW; AFE4AC2931468554 CRC64;
MFHQAKWDEP TIFELSRPGR IGYTLPKPIE DVDVDIPEKL RRKSPLNLPE LSEPEVVKHY
TRLSEMNYGV DSGIYPLGSC TMKYNPKINE EIASHPGVAY VHPYQDEGTV QGALKIMWEL
EQWLKEITGM DRFTLQPAAG ANGEFTGVSI IRAYHIDRGE TQRTEMLVPD SAHGTNPASA
AMAGFKVIEI PSNENGTVDL EALENAVSER TAGLMLTNPN TLGIFEDEIL EIAKIVHKAG
GLLYYDGANL NAVLGKIRPG DMGFDVVHLN LHKTFSTPHG GGGPGSGPVG VKDFLKDYLP
VPLVSYDAEN DRYYLDYNVP RSIGKVKELY GNFAVIVRAL TYLKIMGREG LKEVSEVAVL
NANYLTQKLK GTRGYELPGK ELRKHETVFS AEPMKKETGV KALDVAKRLL DFCMHAPTIY
FPLIVHEALM IEPTETVSKE ELDAYVEALK RISEEAYSNP EVVTSAPHNT AVRRVDDVLA
AKKPVITWRM YRELKERGEI DY
//
