ID A0A3M8FNM6_9BACT Unreviewed; 964 AA.
AC A0A3M8FNM6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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:RNC79349.1};
GN ORFNames=ED557_14800 {ECO:0000313|EMBL:RNC79349.1};
OS Balneola sp.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Balneola.
OX NCBI_TaxID=2024824 {ECO:0000313|EMBL:RNC79349.1, ECO:0000313|Proteomes:UP000280416};
RN [1] {ECO:0000313|EMBL:RNC79349.1, ECO:0000313|Proteomes:UP000280416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bin6 {ECO:0000313|EMBL:RNC79349.1};
RA Zheng Q., Wang Y., Jiao N.;
RT "Metagenomics and metaproteomics analyze the interactions between
RT Synechococcus and associated heterotrophic bacteria in one oligotrophic
RT Synechococcus culture.";
RL Submitted (OCT-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RNC79349.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RHLJ01000007; RNC79349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8FNM6; -.
DR Proteomes; UP000280416; Unassembled WGS sequence.
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; 2.
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:UP000280416}.
FT DOMAIN 13..439
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 468..737
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 779..900
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 707
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 964 AA; 106312 MW; BFCB360864D29CA2 CRC64;
MSIHFEKEQF ASRHNGSNIS ATSEMLETVK ADNLDQLIDE TIPKEIRLSQ GLDLPEALSE
VEFLEEFKKL ASKNRVFKSF IGMGYYDTHV PNVIKRNILE NPAWYTAYTP YQAEIAQGRL
EALINFQTMV SDLTGMELAN ASLLDEGTAA AEAMSMLLGV RKGAKRKEAH DFFVSEHCHP
QTIEVLQTRA EPIGVNIIVG DHNELDVTNP ALYGILLQYP ASNGSVEDYS NLITAAHENQ
VRVVVAADLL SLTLLTPPGE MGADIVVGTT QRFGVPMGFG GPHAAYYATK EEFKRQIPGR
IIGVTQDAEG KPAYRMALQT REQHIRREKA TSNICTAQVL LGVMAGMYGV YHGAEGLTRI
ASKVYGLTKL TKAGLQALDV EVETAAFFDT ITVKANEKRI RKVAEANEVN FRYFGDGRVG
ISFDEAKEIE DVELVLSIFA EAEGRVQNFD VRAHSESVSI SLPATLTRTS EFMTHPVFSL
YQTEHEMLRY MKRLENKDLS LVHSMISLGS CTMKLNATAE MIPVTWPEFG QLHPFAPKNQ
AGGYYQLFDE LVEWLSEITG FDSVSLQPNS GAQGEYAGLM TIRAYHKSRG EGHRNIALIP
SSAHGTNPAS AVMAGMDVVV VATDKYGNIS TEDLAEKAEK YSDRLAALMI TYPSTHGVFE
HKVKEFCEII HQHGGQVYMD GANMNAQVGL TSPGEIGADV CHLNLHKTFC IPHGGGGPGM
GPIGVAKHLT PFLSGHSVIE TGGNQGITAI SAAPFGSASI LTISYAYIRM MGANGLTDAT
RYAILNANYI KDRLKDHFPI LYTGKSGRSA HEFIVDLRPF KQTAGIEAVD VAKRLMDYGF
HAPTMSFPVA GTLMIEPTES ESKEELDRFC EAMINIRHEI REIEDGIADQ ESNVLKHAPH
TMRVVMAESW ERSYSREKGA FPIEELRFNK FWPSVSRVDD AYGDRNLICS CIPIDAYEME
EVEG
//
