ID A0A345QDS7_9RHOB Unreviewed; 948 AA.
AC A0A345QDS7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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 ORFNames=C1J02_17170 {ECO:0000313|EMBL:AXI43464.1};
OS Sulfitobacter sp. SK011.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1389004 {ECO:0000313|EMBL:AXI43464.1, ECO:0000313|Proteomes:UP000253968};
RN [1] {ECO:0000313|EMBL:AXI43464.1, ECO:0000313|Proteomes:UP000253968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK011 {ECO:0000313|EMBL:AXI43464.1,
RC ECO:0000313|Proteomes:UP000253968};
RA Pohlner M., Engelen B., Bunk B.;
RT "Comparative analysis of Sulfitobacter strains from the North Sea.";
RL Submitted (JAN-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}.
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DR EMBL; CP025803; AXI43464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345QDS7; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000253968; Chromosome.
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:UP000253968}.
FT DOMAIN 16..439
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 453..727
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 765..886
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 699
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 948 AA; 103175 MW; BB6470C185330596 CRC64;
MTFKPTDYLP YDFANRRHIG PSPAEMSDML KTVGAKSLAA LIDDTLPAAI RTKEPLDFGK
AMSEREVLEH MRITAGKNKV LTSLIGQGYH GTVTPPAIQR NILENPAWYT AYTPYQPEIS
QGRLEALLNF QTMVSDLTGL EIANASLLDE ATACAEAMTM AQRVAKSKAT AFFIDRDCHP
QNIAVMKTRA APLGIDVIVG DPDKMDASAV FGAVFQYPGT YGHVRDFTKH IAALHEANAI
GIISADPLSL TLLKEPGEMG ADIAVGSTQR FGVPEGYGGP HAAYMACKDT MKRAMPGRIV
GVSIDAHGNR AYRLSLQTRE QHIRREKATS NVCTAQALLA VMASMYAVFH GPEGLKAIAQ
RIHRKTVRLA KGLEAAGFKV DPQAFFDTIT VDVGPLQAAV MKSAVDEGIN LRRVGETRVG
ITMDERSRPA TIEAVWRAFG IRQADDDFTP DYRVPDDMLR TSEYLTHPIF HMNRAETEMM
RYMRRLADRD LALDRAMIPL GSCTMKLNSA AEMMPVSWRE FSQMHPFVPA DQALGYKELI
DDLSSKLCDI TGYDAISMQP NSGAQGEYAG LLTIAGYHRA EGQGHRDVCL IPVSAHGTNP
ASAQMVGWKV VVIKSAANGD IDLDDFRAKA EQHSDNLAGC MITYPSTHGV FEETVTEVTK
ITHQHGGQVY IDGANMNAMV GLSRPGDLGG DVSHLNLHKT FCIPHGGGGP GMGPIGVKSH
LIAHLPGHPN EGGAAVSAAP FGSPSLLPIS WAYCLMMGGE GLTQATRVAI LNANYIAKRL
EGAFDVLYKG PTGRVAHECI LDVRPFEDSA GVTVDDIAKR LIDAGFHAPT MSWPVAGTLM
VEPTESENKA ELDRFCDAML AIRDEITAIE KGDMPRENNP LKNAPHTVED LVLEWGDRPY
TREQGCFPPG AFRVDKYWPP VNRVDNVHGD RNLICTCPPL EDYAEAAE
//
