ID A0A3S2Y1F8_9SPHI Unreviewed; 969 AA.
AC A0A3S2Y1F8;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 18-JUN-2025, entry version 24.
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:RVT98347.1};
GN ORFNames=EOD41_16260 {ECO:0000313|EMBL:RVT98347.1};
OS Mucilaginibacter limnophilus.
OC Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
OC Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1932778 {ECO:0000313|EMBL:RVT98347.1, ECO:0000313|Proteomes:UP000282759};
RN [1] {ECO:0000313|EMBL:RVT98347.1, ECO:0000313|Proteomes:UP000282759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YBJ-36 {ECO:0000313|EMBL:RVT98347.1,
RC ECO:0000313|Proteomes:UP000282759};
RA Chen W.-M.;
RL Submitted (JAN-2019) 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=N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage complex H protein]
CC + glycine + H(+) = N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-L-lysyl-
CC [glycine-cleavage complex H protein] + CO2; 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:ARBA00049026, 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:RVT98347.1}.
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DR EMBL; SACK01000008; RVT98347.1; -; Genomic_DNA.
DR RefSeq; WP_127706850.1; NZ_SACK01000008.1.
DR AlphaFoldDB; A0A3S2Y1F8; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000282759; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:TreeGrafter.
DR GO; GO:0016594; F:glycine binding; IEA:TreeGrafter.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:TreeGrafter.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR CDD; cd00613; GDC-P; 2.
DR FunFam; 3.40.640.10:FF:000005; Glycine dehydrogenase (decarboxylating), mitochondrial; 1.
DR FunFam; 3.40.640.10:FF:000007; glycine dehydrogenase (Decarboxylating), mitochondrial; 1.
DR FunFam; 3.90.1150.10:FF:000007; Glycine dehydrogenase (decarboxylating), mitochondrial; 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 NCBIfam; NF001696; PRK00451.1; 1.
DR NCBIfam; NF003346; PRK04366.1; 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|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00711}; Reference proteome {ECO:0000313|Proteomes:UP000282759}.
FT DOMAIN 14..436
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 443..737
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 778..898
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 706
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 969 AA; 106405 MW; 84D8C63749614136 CRC64;
MQLNTDYQEK FQFRHIAPNE ADTAEMLKTV GVNSIDELIE QTIPAPIRLK QPLNLPPAKS
EFDYLNTLKQ TASRNKVFKS YIGQGYYDVI VPGVIQRNIL ENPGWYTQYT PYQAEIAQGR
LQALLNFQTM VIDLTGMEIA NASLLDEGTA AAEAMFMQYS LRKNQKATKF FVSDELFAQT
IDILKTRSEP FGIELVIGSH ENVELSDDMF GAIVQYPAKN GEVYDYKDFA AKAHEKGIKL
TVVADLMSLV LLTPPGEWGA DIVVGTSQRF GIPMGFGGPH AAFFATKEEY KRSMPGRIIG
VTIDSANNYA LRMALQTREQ HIRRDKATSN ICTAQALLAI MAGMYAAYHG PKGLKLIAER
IHGLTVLLSN SLEELGYKQL NTAYFDTLQF DLGELVGPLH GEALNNEMNL NYNGSIVTIS
LDETTSPEDV KTIVRFFAKV KGKNLNDVNI DELKSNLQTT IPAALQRTSA YLTHPVFNSH
HSEHEMLRYI KSLETKDLSL CHSMIALGSC TMKLNATTEM VPVTWAEFSR IHPFAPVDQT
GGYMQLFAEL DAWLSEITGF AAMSLQPNAG AQGEYAGLMV IRAYHNDRGD THRNIALIPS
SAHGTNPASA AMAGMKIVVV KCDDNGNIDV ADLKAKAEQY KNELSCLMVT YPSTHGVFEE
SIIEVCEIIH ANGGQVYMDG ANMNAQVGLT SPATIGADVC HLNLHKTFCI PHGGGGPGMG
PIGVAKHLVP YLPGHAVVDI DKGKSIPAVS AAPWGSASIL IISHAYIAMM GGEGLTSATK
YAILNANYIK TRLKAHYPVL YTGSKGRCAH EMILDCRAFK AYGIEVTDIA KRLMDYGFHA
PTVSFPVAGT VMIEPTESEP KHELDRFCDA MIAIRNEIKD VESGVSDKTD NPLKNAPHTA
AVVTGNDWEH PYTRQKAAFP LPYVAAYKFW PSVGRVNDTY GDRTLICSCP PLTEYEFEES
EVTTPEFGT
//
