ID A0A1N7SQK7_9BURK Unreviewed; 976 AA.
AC A0A1N7SQK7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, 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 ECO:0000313|EMBL:SIT49632.1};
GN ORFNames=BN2476_700024 {ECO:0000313|EMBL:SIT49632.1};
OS Paraburkholderia piptadeniae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1701573 {ECO:0000313|EMBL:SIT49632.1, ECO:0000313|Proteomes:UP000195569};
RN [1] {ECO:0000313|EMBL:SIT49632.1, ECO:0000313|Proteomes:UP000195569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM 7183 {ECO:0000313|EMBL:SIT49632.1,
RC ECO:0000313|Proteomes:UP000195569};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-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}.
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DR EMBL; CYGY02000070; SIT49632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7SQK7; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000195569; 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}.
FT DOMAIN 28..454
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 492..766
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 797..918
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 724
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 976 AA; 105167 MW; 070A52EF20EE7E4A CRC64;
MKLEHPDHLM NRTPLSLAAL EVHDAFAERH IGPDAADQQS MLEALGFASR AALMDAVIPK
TIRRQDALPL GPFAQPKSEA EALAALRELA DKNQVFRSYI GQGYYNAHTP AVILRNVLEN
PAWYTAYTPY QPEISQGRLE ALLNFQQMII DLTGLTISNA SLLDEATAAA EAMTLLQRVG
KPKSNIFYVA DDVLPQTIEV LKTRAKPVGI EVKVGPAADA ANANAFGVLL QYPGVDGDVR
DYRTLADAIH AAGGHVVAAA DLLALTMLTP PGEWGADVAV GNSQRFGVPV GFGGPHAAYL
AVRDEFKRQM PGRLVGVTVD AQGNPALRLA LQTREQHIRR EKATSNVCTA QALLAIMASM
YAVYHGPRGL KTIAQRVNRI AALLAEGAKQ LGYTLVNETF FDTLTFETGA RTQALHDAAT
AKRINLRHVS DTRVGISIDE TTTRADLADL LAAFAQAAFV SDVPQIDELD AKLGQSNTFP
ATLERESAYL THHVFNRHHS ETEMLRYLRS LADKDLALDR SMIPLGSCTM KLNATSEMLP
VTWPEFGQIH PFAPAQQTVG YREMIDQLEQ MLVAATGYAA VSLQPNAGSQ GEYAGLLIIH
AYHESRGEGH RNVCLIPASA HGTNPASAHM AGMQVVVVAC DAQGNVDIED LKKKAGQHAD
KLAAIMITYP STHGVFEQNV REICEIVHAH GGQVYVDGAN MNAMVGLTAP GQFGGDVSHL
NLHKTFCIPH GGGGPGVGPV AVGAHLAKFL PNQTSTGYER DANGIGAVSA APYGSASILP
ISWMYIAMMG AKNLTAATEA AILNANYVAK KLAPHYPVLY SGPGGLVAHE CILDLRPIKE
TSGISVDDVA KRLMDYGFHA PTMSFPVPGT LMVEPTESES KEELDRFIEA MIAIRNEIRA
VEEGRSDRED NPLKHAPHTA AVVVANEWAH GYARETAAYP LPSLVAKKYW PPVGRADNAY
GDRNLFCSCV PMADYE
//
