ID A0A0M4QZG9_9MICC Unreviewed; 948 AA.
AC A0A0M4QZG9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000256|HAMAP-Rule:MF_00711};
DE EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine cleavage system P-protein {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine decarboxylase {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|HAMAP-Rule:MF_00711};
GN Name=gcvP {ECO:0000256|HAMAP-Rule:MF_00711};
GN ORFNames=AOC05_04570 {ECO:0000313|EMBL:ALE93998.1};
OS Arthrobacter alpinus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=656366 {ECO:0000313|EMBL:ALE93998.1, ECO:0000313|Proteomes:UP000062833};
RN [1] {ECO:0000313|Proteomes:UP000062833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R3.8 {ECO:0000313|Proteomes:UP000062833};
RA See-Too W.S., Chan K.G.;
RT "Complete genome of Arthrobacter alpinus strain R3.8.";
RL Submitted (SEP-2015) 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. {ECO:0000256|ARBA:ARBA00003788, ECO:0000256|HAMAP-
CC Rule:MF_00711}.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00043839, ECO:0000256|HAMAP-
CC Rule:MF_00711};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00711, ECO:0000256|PIRSR:PIRSR603437-50};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000256|ARBA:ARBA00011690, ECO:0000256|HAMAP-
CC Rule:MF_00711}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC ECO:0000256|HAMAP-Rule:MF_00711}.
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DR EMBL; CP012677; ALE93998.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M4QZG9; -.
DR KEGG; aaq:AOC05_04570; -.
DR PATRIC; fig|656366.3.peg.984; -.
DR Proteomes; UP000062833; Chromosome.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR CDD; cd00613; GDC-P; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR HAMAP; MF_00711; GcvP; 1.
DR InterPro; IPR003437; GcvP.
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 NCBIfam; TIGR00461; gcvP; 1.
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; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00711};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00711,
KW ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000062833}.
FT DOMAIN 7..435
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 469..731
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 767..888
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 698
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 948 AA; 100665 MW; 49A2F14DC32D8F82 CRC64;
MSAAFTDRHI GVSTQPHVHH MLSALGFGSL EELSVAALPE SIYITEPLSL QAAVSEEAML
VELKALAAKN TVNKSFIGQG YYGTHTPGVI QRNVLESPAW YTAYTPYQPE ISQGRLEALL
NFQTVVSDLA GMVTANASML DEGTAAAEAM ALMRRTNRTA KSDAVFLVDA DVFPQTLAVI
NTRAKAMGIP VLVHDFDAEL PDVECFGVLL QYPGDSGRIR QIAPIIEAAH ARKAVVGVAA
DLLALTLLES PGALGADLAV GSSQRFGVPM GFGGPHAGYM SVRAGLERSL PGRLVGVSKD
AAGNQAYRLA LQTREQHIRR EKATSNICTA QVLLAVMAGM YAVYHGPEGL RKIARRVHAM
AQSVAQAAMA AGHTVVHANY FDTVKIAVAA GSGHSAAELV AAAHSAGYLL RQVDHGHIQI
AVDETTIEAD VAALAGLLGA TALELAPDAS AVVLPTPVRA TGYMGNAVFH AHNSETQMLR
YLRKLSDADY ALDRGMIPLG SCTMKLNATA EMAGVTWPEF STLHPYAPAS DTVGIVEMAT
QLESWLAEIT GYDAVSVQPN AGSQGEFAGL MAIRAYHVEN GNPERDIVLI PTSAHGTNAA
SAVMAGLKVV AVATDGFGNI DIDDLKRQIT VHEHRLAAIM VTYPSTHGVF ETSISTICAM
VHDAGGQVYV DGANLNALVG LAQPGKFGAD VSHLNLHKTF CIPHGGGGPG VGPVAVGVHL
AKHLPARELG LETSVGLVSS APYGSASILP ISWAYIRMMG PEGLRLATQT AILSANYIAR
RLSEHYPVLY TGAHDLVAHE CILDLRGITA DSGVTVDDVA KRLIDYGFHA PTMSFPVAGT
LMVEPTESED LGEIDRFINA MISIRMEISA VQDGLWPADD NPLVNAPHTA QCLTQDWDHP
YSREDAVFPA GVDPRAKYWP IVRRIDQAYG DRHLVCSCPS IEELAEVF
//
