ID A0A9X2BED5_9SPHI Unreviewed; 969 AA.
AC A0A9X2BED5;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
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:MCJ8211293.1};
GN ORFNames=MUY27_16360 {ECO:0000313|EMBL:MCJ8211293.1};
OS Mucilaginibacter straminoryzae.
OC Bacteria; Pseudomonadati; Bacteroidota; Sphingobacteriia;
OC Sphingobacteriales; Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=2932774 {ECO:0000313|EMBL:MCJ8211293.1, ECO:0000313|Proteomes:UP001139450};
RN [1] {ECO:0000313|EMBL:MCJ8211293.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RS28 {ECO:0000313|EMBL:MCJ8211293.1};
RA Ko S.-R.;
RT "Mucilaginibacter sp. RS28 isolated from freshwater.";
RL Submitted (APR-2022) 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:MCJ8211293.1}.
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DR EMBL; JALJEJ010000009; MCJ8211293.1; -; Genomic_DNA.
DR RefSeq; WP_245131782.1; NZ_JALJEJ010000009.1.
DR AlphaFoldDB; A0A9X2BED5; -.
DR Proteomes; UP001139450; 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:UP001139450}.
FT DOMAIN 14..436
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 445..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; 106426 MW; 303633ECB63908E3 CRC64;
MSININYQEE FSSRHIAPNA ADTAKMLKTI GVDSIDQLID QTVPAQIRLK KPLNLPTPKS
ESDYLNTLKQ TASKNRVFKS FIGQGYYDVL VPGVIQRNIL ENPGWYTQYT PYQAEIAQGR
LQALLNFQTM VIDLTGMEIA NASLLDEGTA AAEAMFMQYS LRKNQQANVF FVSEELFPQT
IDILKTRSEP FGIELQIGDH RTAELTDNMF GAIVQYPAGD GTVYNYKDFA AKAHEKNIKL
TVVADIMSLL LLTPPGEWGA DIVVGTTQRF GVPMGFGGPH AAYFATKEEY KRSMPGRIIG
VTIDSAGDYA LRMALQTREQ HIRRDKATSN ICTAQALLAI MAGMYAVYHG PEGLKLIAER
IHGLAILLAK SLEKLGYKQL NEAYFDTVKF DVGNLAGPIH GEALNNEMNL HYNGSVISIA
LDETTRVQDI ETIVRFFAKV KGKTINDVDF EGLKSGIETV IPQDLQRTSA YLTHAIFNSH
HSEHEMLRYI KALEAKDLSL THSMIPLGSC TMKLNATTEM IPVTWAEFGK LHPFAPTDQV
GGYMQVFNEL NAWLSEITGF AAMSLQPNAG AQGEYAGLMV IRAYHQDRGD SHRNIALIPS
SAHGTNPASA AMAGMKIVVV KCDENGNIDV ADLKARAEQY KNELSCLMVT YPSTHGVFEE
SIIEICEIIH QNGGQVYMDG ANMNAQVGLT SPATIGADVC HLNLHKTFCI PHGGGGPGMG
PIGVAAHLVP YLPGHAVVDI DQGKSIHAVS AAPWGSASIL LISHAYIAMM GGEGLTNATK
YAILNANYIK SRLENHYPVL YTGSQGRCAH EMILDCRAFK NFGIEVVDIA KRLMDYGFHA
PTVSFPVAGT VMVEPTESEP KHELDRFCDA MIAIRKEIED VENGKSDKTD NPLKNAPHTS
AVVTGNEWEH PYTRQKAAFP LPYVAAHKFW PSVGRVNDTY GDRTLICSCP PLSEYEFEEA
EVTTPEYGT
//
