ID A0A0L6CTM3_9RHOB Unreviewed; 949 AA.
AC A0A0L6CTM3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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:KNX40858.1};
GN ORFNames=ROTO_26110 {ECO:0000313|EMBL:KNX40858.1};
OS Roseovarius tolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=74031 {ECO:0000313|EMBL:KNX40858.1, ECO:0000313|Proteomes:UP000037046};
RN [1] {ECO:0000313|Proteomes:UP000037046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EL-164 {ECO:0000313|Proteomes:UP000037046};
RA Voget S., Bruns H., Wagner-Doebler I., Schulz S., Daniel R.;
RT "Draft Genome Sequence of Roseovarius tolerans EL-164, a producer of N-
RT Acylated Alanine Methyl Esters (NAMEs).";
RL Submitted (JUL-2015) 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:KNX40858.1}.
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DR EMBL; LGVV01000038; KNX40858.1; -; Genomic_DNA.
DR RefSeq; WP_050663476.1; NZ_LGVV01000038.1.
DR AlphaFoldDB; A0A0L6CTM3; -.
DR STRING; 74031.SAMN04488077_105206; -.
DR PATRIC; fig|74031.6.peg.2663; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000037046; 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:UP000037046}.
FT DOMAIN 16..439
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 455..727
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 767..888
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 949 AA; 103703 MW; 36FEBC364082311E CRC64;
MPFKATDYLP YDFANRRHIG PSPEEMGEMF EVLGVETLEA LIDETVPKSI RQEAPLDFGK
PKSESELLHH MWQTASKNKV LTSLIGQGYH GTVTPPAIQR NIFENPAWYT AYTPYQPEIS
QGRLEALLNF QTMVSDLTGL EIANASLLDE ATAAAEAMTM AQRVAKSKAR AFFVDENCHP
QNIAVMQTRA APLDIEVIVG APEEMEASKV FGAIFQYPGT HGGLRDFSAE IAALHEGKAI
GIVIADPLAL TLLKEPGAMG ADIAVGSTQR FGVPVGYGGP HAAYMATKDA YKRALPGRIV
GVSVDSHGNR AYRLSLQTRE QHIRREKATS NVCTAQALLA VMASMYAVFH GPKGLRAIAQ
RIHRKTVRLA KGLEAAGFHV EPGDFFDTIT VDVGLLQRGV LQSAVREGVN LRRVGDTKIG
ITLDERTRTK TVEAVWRAFG IIMEDSDFTP EYRIPEVLQR ESAYLTHPIF HMNRAETEMM
RYMRRLADRD LALDRAMIPL GSCTMKLNSA AEMMPVSWRE FSLLHPFVPA DQALGYKEMI
DDLSAKLCDI TGYAAISMQP NSGAQGEYAG LLSIAAYHRA NGEGHRKVCL IPVSAHGTNP
ASAHMVGWDV VVVKSADNGD IDVEDFRAKA EKHSDNLAGC MITYPSTHGV FEETVRDVCA
ITHEHGGQVY IDGANMNAMV GLARPGDVGG DVSHLNLHKT FCIPHGGGGP GMGPIGVKAH
LVPHLPGHPA TGGEEGPVSA APYGSPSLLP ISWAYCLMMG GAGLTQATRV AILNANYIAK
RLEGAYDVLY KGPTGRVAHE CILDTRPFEK SAGVTVDDIA KRLMDCGFHA PTMSFPVPGT
LMVEPTESET KAELDRFIDA MLAIRQEIRD IEEGRMEAEN NPLKNAPHTM EDLIREWDRP
YSREQGCFPP GAFRVDKYWP PVNRVDNVYG DRHLICTCPP LEDYAEAAE
//
