ID A0A432DK49_9BURK Unreviewed; 967 AA.
AC A0A432DK49;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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:RTZ40629.1};
GN ORFNames=EKL30_16005 {ECO:0000313|EMBL:RTZ40629.1};
OS Candidimonas sp. SYP-B2681.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Candidimonas.
OX NCBI_TaxID=2497686 {ECO:0000313|EMBL:RTZ40629.1, ECO:0000313|Proteomes:UP000288599};
RN [1] {ECO:0000313|EMBL:RTZ40629.1, ECO:0000313|Proteomes:UP000288599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SYP-B2681 {ECO:0000313|EMBL:RTZ40629.1,
RC ECO:0000313|Proteomes:UP000288599};
RA Zhang M.-Y., Zhang Y.-X.;
RT "Candidimonas lamiisoli sp. nov., a novel bacterium can accelerate seed
RT germination.";
RL Submitted (DEC-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:RTZ40629.1}.
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DR EMBL; RYDV01000008; RTZ40629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432DK49; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000288599; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000288599}.
FT DOMAIN 14..435
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 475..731
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 776..897
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 702
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 967 AA; 103342 MW; 05F391F87C7D8F24 CRC64;
MLRELDPHSD FIPRHIGPSA ADQAKMLSAI GVDDLHSLIQ EVVPPSILKR GALNLPASRS
EADALAELKE IAGRNQVFRN YIGQGYYGTQ VPNVILRNIL ENPAWYTAYT PYQPEISQGR
LEALLNYQTM VADLTGLDIA NASLLDEGTA AAEAMGLARR SAKSKSNVFF ASVHCHPQTI
EILRTRAIGL DIDVLVGDEA QGLPECFGVL LQYPHSLGGL ADYRGLTEAA HAQGAVVAVA
TDLLALALLT PPGEWGADIA IGSAQRFGVP LGFGGPHAGF MSCKDAFKRN MPGRLVGVSK
DSQGAPALRL ALQTREQHIR REKATSNICT AQVLLAVMAG MYAVWHGPAG LKRIAERVAY
LTAFLRKSLT DLGISVVNQQ YFDTLLLDTG AQTAAIIKSA QDASINLRQV GSHQLAVSLD
ETVTVADLHA LLQVFAQATG KSWNPEDSHT LPAKHGISAG LLRQSAILSH PVFSQIRSET
DMLRYLRTLA DKDLALDRSM IPLGSCTMKL NATAEMIPIT WPEFSNMHPF APASQAQGYK
ELIDRLSAAL CEITGYDSIS LQPNSGAQGE FAGLLAIRAY HQANGQHQRN VCLIPASAHG
TNPASAQLAG MEVVVVASDD NGNVDVSDLK AKIAKVGDRL AALMITYPST HGVFEVAITE
ICALIHDAGG QVYLDGANMN AMVGLAQPGK FGSDVSHLNL HKTFCIPHGG GGPGVGPVAV
RSHLAPYLPG ILNESGELPA HTPVGPVSAA PYGSASILPI PYLYITLMGV EGLLAATEVA
ILNANYIAAR LQGHYPILYA GHHGRVAHEC ILDVRPIKDS CGISAEDIAK RLIDYGFHAP
TMSFPVAGTL MVEPTESEGL AELDRFIDAM IAIRAEIAAI ESGAKDAQDN VLKNAPHTAQ
MLLVTEWHHD YTREEAAYPV GSLRSTKYWS PVARVDNAYG DRNLICSCPP LEDYVDESDT
TAVQPAA
//
