ID A0A3S8Z6L0_9ACTO Unreviewed; 967 AA.
AC A0A3S8Z6L0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 ECO:0000313|EMBL:AZN29088.1};
GN ORFNames=EJO69_01320 {ECO:0000313|EMBL:AZN29088.1};
OS Flaviflexus salsibiostraticola.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Flaviflexus.
OX NCBI_TaxID=1282737 {ECO:0000313|EMBL:AZN29088.1, ECO:0000313|Proteomes:UP000270021};
RN [1] {ECO:0000313|EMBL:AZN29088.1, ECO:0000313|Proteomes:UP000270021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 33148 {ECO:0000313|EMBL:AZN29088.1,
RC ECO:0000313|Proteomes:UP000270021};
RA Bae J.-W.;
RT "Complete genome sequence of Flaviflexus salsibiostraticola KCTC 33148.";
RL Submitted (DEC-2018) 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; CP034438; AZN29088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S8Z6L0; -.
DR KEGG; fsl:EJO69_01320; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000270021; 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; 1.
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:UP000270021}.
FT DOMAIN 13..435
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 776..897
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 697
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 967 AA; 102859 MW; 74A27DAACF88C713 CRC64;
MRRGAAVTSF QPRHIGTWGS DRSAMLARVG VGSLDELMEA ALPAGLTREA LDGLPGGRSE
QDVLERLSDL AAKNTVRISM IGQGYYDTVT PAVIRRNILE NPSWYTAYTP YQPEISQGRL
EALVNFQTMV SDLTGMDIAN SSMLDEATAV AEAMLLACRV ARSRTRVLIA EDVFDATRAV
VETRAGALGI ELTESDFSQI DDDVAAVILQ YPGASGHLPE LSELEAITAR AHASGALVVV
AADLLSLSLL ASPGSWGADL VAGSTQRFGV PMAGGGPHAG YLAVKDAHKR QLPGRLVGVS
KDADGAVAYR LALQTREQHI RREKATSNIC TAQVLLAVMA STYAVYHGPD GLRRIAERVH
DHAVSLAERL ARAGVPVTST SFFDTVELEI PDGADRALRH LLAENITGWR VDESTIRLSC
DEKTTGEVID RVVRALEASG TEADKTGIDA GFPSSLERRD DYLTHPTFHR YRTETLLMRY
LKALADKDYA LDRGMIPLGS CTMKLNSAIE MSPITWPGFA FIHPFAPATD RLGYLELIED
LETWLAAVTC YDAVSLQPNA GSQGELAGLL AIRGYHRSRG DTERTVCLIP ASAHGTNAAS
AVLAGFRVVV VGTGPDGSVS LTDLDAKISE YEDQLGAIMI TYPSTHGIYE DSVGEVCARV
HAAGGQVYID GANLNALVGV ARPGDFGGDV SHLNLHKTFA IPHGGGGPGV GPVAAQSHLV
PFLPSHPMTD NSVIGSASAI TPGAGAVSQA PYGSAGILPI SYAYILLMGG EGLMTATQSA
VLAANYVAAK VDKVLPVLYR GPGGLVGHEC IIDLRPLREE TGITVDDVAK RLIDYGFHAP
TMSFPVAGTL MIEPTESEDL GEIDRLCDAL LKIHDEARSV YEGTWPQDDN PLVNAPHTAA
SALVGEWSHP YSRAVAVYPA LAEDVLDDPA QLAAAAAGKY WPPVRRIDGP FGDRNLVCSC
PPIESCR
//
