ID A0A1B6Y620_9BACT Unreviewed; 965 AA.
AC A0A1B6Y620;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=A8B79_10660 {ECO:0000313|EMBL:OAN60398.1};
OS Balneola sp. EhC07.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Balneola.
OX NCBI_TaxID=1849360 {ECO:0000313|EMBL:OAN60398.1, ECO:0000313|Proteomes:UP000078514};
RN [1] {ECO:0000313|EMBL:OAN60398.1, ECO:0000313|Proteomes:UP000078514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EhC08 {ECO:0000313|EMBL:OAN60398.1,
RC ECO:0000313|Proteomes:UP000078514};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) 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:OAN60398.1}.
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DR EMBL; LXYG01000019; OAN60398.1; -; Genomic_DNA.
DR RefSeq; WP_066223815.1; NZ_LXYG01000019.1.
DR AlphaFoldDB; A0A1B6Y620; -.
DR STRING; 1849360.A8B79_10660; -.
DR InParanoid; A0A1B6Y620; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000078514; 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:UP000078514}.
FT DOMAIN 12..439
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 461..729
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 965 AA; 106571 MW; 3A48AAC3B2E257F5 CRC64;
MNISFEKETF AHRHNGNDPE AITEMLKTIK AESIDQLIDE TIPENIRLQE KLNLPKAQSE
VDFLAGFKKL ASKNKIFKSY IGMGYYDTHV PNVIKRNILE NPAWYTAYTP YQAEIAQGRL
EALINFQTLV SDLTGMELAN ASLLDEGTAA AEAMSMLLGQ RKGAKRKEAN VIFVSDRCHP
QTIDVLQTRA EPIGIEVVVG DHNEVDVTDP KLFALLLQYP ATDGSVIDYT SLIAAAHENA
VHAVVAADLM SLTLLTPPGE MGADVVVGTT QRFGVPMGYG GPHAAYFATK EDFKRQIPGR
IIGVTQDAEG KPAYRMALQT REQHIRREKA TSNICTAQVL LAVMAGMYGV YHGPKGLKKI
ASKIHGLTKL TKSGLEAMGV SVETDMFFDT ITVKASEKKV RKIAEENEIN FRYLGDNRIG
ISFDEAKELE DVQEVLSVFA KAEGRTSNFD VEAHAEKAEV KLPEELARTS EYLDHPVFNL
YHTEHEMLRY MKRLENKDLS LVHSMISLGS CTMKLNATAE MIPVTWPEFG QMHPFAPVEQ
AEGYTQLFNE LDEWLSSLTG FHKVSMQPNS GAQGEYAGLM TIRAYHQSKG DDHRNVALIP
NSAHGTNPAS AVMAGMDVIV VDTDKHGNIS MDDLEAKTIK YSDRLAALMV TYPSTHGVFE
HRIKDICDLI HEHGGQVYMD GANMNAQVGL TSPGFIGADV CHLNLHKTFC IPHGGGGPGM
GPIGVAEHLA PFLSSHAVIK TGGESGISAV SAAPYGSASI LTISYAYIAM MGESGLTEAT
RMAILNANYI KDILDDHYPI LYTGKTGRSA HEFIIDLRPF KQSAGIEAVD LAKRLMDFGF
HAPTMSFPVA GTLMIEPTES ESKEELDRFC DAMIEIRNEI REIEEGKADK ESNVLKHAPH
TMRVVMDSDW DRDYDREKGV FPLEHLRENK FWPSVSRVDD AYGDRNLMCS CIPIDAYAIE
EIEGE
//
