ID A0A3N4ANM2_9PSED Unreviewed; 961 AA.
AC A0A3N4ANM2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=EF099_04780 {ECO:0000313|EMBL:ROZ85632.1};
OS Pseudomonas sp. SSM44.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2487347 {ECO:0000313|EMBL:ROZ85632.1, ECO:0000313|Proteomes:UP000268556};
RN [1] {ECO:0000313|EMBL:ROZ85632.1, ECO:0000313|Proteomes:UP000268556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSM44 {ECO:0000313|EMBL:ROZ85632.1,
RC ECO:0000313|Proteomes:UP000268556};
RA Jang G.I., Hwang C.Y.;
RL Submitted (NOV-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:ROZ85632.1}.
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DR EMBL; RKKV01000003; ROZ85632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4ANM2; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000268556; 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; 1.
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:SF13; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 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:UP000268556}.
FT DOMAIN 18..440
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 464..731
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 782..903
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 709
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 961 AA; 104150 MW; E00D5B7EB5C0022E CRC64;
MSNAFSLTDL EQTDDFIRRH IGPDAAEQQA MLDALGANSL EDLVGQTVPQ SILRNELLEL
GAPRSEAEVL SYLKQVAARN QVFTSCIGMG YHGTLTPTVI LRNVLENPGW YTAYTPYQPE
IAQGRLESLL NFQQLTIDLT GMELASASLL DEATAAAEAM ALAKRVAKSK SNLFFVDEDC
HPQTISVVLT RAEAFGFDVV VDDVSTLGEH EVFGALFQYP TTWGEIRDLK PLIERVQAQK
GLACVSADLL ALVKLTSPGE LGADVVFGSA QRFGVPMGYG GPHAAFFATR DAYKRAMPGR
IIGVSVDARG NRALRMALQT REQHIRREKA NSNICTAQVL LANIASFYAV YHGPQGLKVI
ADRVHRLTAI LAAGLQAAGV TLRNQSFFDT LTLNVPGKAG EIVGRARAAR VNLRMIDGDA
VGVSLDETTT RATVETLLAV IVGEAHGQNL SALDAQIIGT EPGIPAELRR TSDFLTHPVF
NSYHSETEML RYIKSLENKD LALNHSMIPL GSCTMKLNAT TEMIPITWPE FGQLHPFVPL
AQAEGYKQMI DELEAMLRGI TGFDAICMQP NSGAQGEYAG LLAIRKFHEA NGDAHRDVCL
IPTSAHGTNP ASAMMASMRV VLVACDDQGN VDVADLRQKA EDNAEKLSCL MITYPSTHGV
YEEGIREICE IVHQHGGQVY MDGANLNAQV GLTRPADIGA DVSHMNLHKT FCIPHGGGGP
GMGPIGVKAH LAPFVANHPV VPLDGPNPQN GAVSAAPWGS ASILPISWTY IALMGAIGLR
QATAVAILNA NYLAKRLGDA YPVLYSGRNG RVAHECIIDI RPLKAASGIT EEDVAKRLMD
FGFHAPTMSF PVAGTLMIEP TESESKAELD RFVDAMLTIR AEIRKVEQGE WTAEDNPLHN
APHTLADITG DWQRAYSREE AVFPQAWVAA NKFWPSVNRI DNVYGDRNLF CACPPIESYE
D
//
