ID A0A3D8JZX5_9BURK Unreviewed; 985 AA.
AC A0A3D8JZX5;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 18-JUN-2025, entry version 25.
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:RDU98440.1};
GN ORFNames=DWV00_14165 {ECO:0000313|EMBL:RDU98440.1};
OS Trinickia dinghuensis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Burkholderiaceae; Trinickia.
OX NCBI_TaxID=2291023 {ECO:0000313|EMBL:RDU98440.1, ECO:0000313|Proteomes:UP000256838};
RN [1] {ECO:0000313|EMBL:RDU98440.1, ECO:0000313|Proteomes:UP000256838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHOM06 {ECO:0000313|EMBL:RDU98440.1,
RC ECO:0000313|Proteomes:UP000256838};
RA Gao Z.-H., Qiu L.-H.;
RT "Paraburkholderia sp. DHOM06 isolated from forest soil.";
RL Submitted (AUG-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=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:RDU98440.1}.
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DR EMBL; QRGA01000007; RDU98440.1; -; Genomic_DNA.
DR RefSeq; WP_115534195.1; NZ_QRGA01000007.1.
DR AlphaFoldDB; A0A3D8JZX5; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000256838; 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; 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:UP000256838}.
FT DOMAIN 28..454
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 501..760
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 806..927
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 733
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 985 AA; 105609 MW; 054C0F513FE48D2D CRC64;
MKLEHPDRLM NRSPLSLAAL EVHDAFAERH IGPDGTDQHK MLEVLGFESR AALIDAVIPR
AIRRTDPLPL GSFAEPRSEA EAIACLRELA DKNEVFRSYI GQGYYNTHTP AVILRNVLEN
PAWYTAYTPY QPEISQGRLE ALLNFQQMIG DLTGLEISNA SLLDEATAAA EAMTLLQRAG
KSKSNVFYVA DDVLPQTIEV VRTRAEPIGI DVQVGPADAA AGANAFGVLL QYPGAGGDVR
DYRALTEAVH AAGGHVVVAA DLLALTLLTP PGEWGADVAV GTSQRFGVPV GFGGPHAAYM
AVRDEFKRQM PGRLVGVTVD AQGKSALRLA LQTREQHIRR EKATSNVCTA QALLAIMASM
YAVYHGPHGL KTIAQRVHRV AALLGAGVKQ LGYTLVNETF FDTLTIETGS RTAAVHEAAK
RLRVNLRRVS DTRVGISVDE TTKRADLADL LSLFASAAGA IDVPHVDTLD TALTRGQEQG
QGGDMAAVPA ALVRTSAYLT HHVFNRHHSE TEMLRYLRGL ADKDLALDRS MIPLGSCTMK
LNATSEMLPV TWPEFSQIHP FAPAEQTVGY REMIDQLEQM LVAATGYAAV SLQPNAGSQG
EYAGLLIIHA YHASRGEGHR DVCLIPASAH GTNPASAHMA GMKVVVVACD DQGNVDIADL
KAKAAEHAAK LAAIMITYPS THGVFEQNVR EICEIVHAHG GQVYVDGANM NAMVGLTAPG
QFGGDVSHLN LHKTFCIPHG GGGPGVGPVA VGPHLAQFLP NQTSSGYRRA ESGIGAVSAA
PYGSASILPI SWMYVAMMGA KNLTAATEVA ILNANYVAKR LAPHFPVLYA GPGGLVAHEC
ILDLRPIKDA SGITVDDVAK RLADYGFHAP TMSFPVPGTL MVEPTESESK EELDRFIEAM
IAIRDEIRAV EEGRADREDN PLKHAPHTAA VVTANEWPHA YSREAAAYPL PSLVVRKYWP
PVGRADNAYG DRNLFCSCVP ISDYA
//
