ID A0A2S8RYK9_9RHOB Unreviewed; 949 AA.
AC A0A2S8RYK9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=LX70_03931 {ECO:0000313|EMBL:PQV53611.1};
OS Defluviimonas denitrificans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Defluviimonas.
OX NCBI_TaxID=404881 {ECO:0000313|EMBL:PQV53611.1, ECO:0000313|Proteomes:UP000238338};
RN [1] {ECO:0000313|EMBL:PQV53611.1, ECO:0000313|Proteomes:UP000238338}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18921 {ECO:0000313|EMBL:PQV53611.1,
RC ECO:0000313|Proteomes:UP000238338};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (FEB-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:PQV53611.1}.
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DR EMBL; PVEP01000014; PQV53611.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8RYK9; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000238338; 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:UP000238338}.
FT DOMAIN 16..439
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 465..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; 103161 MW; D40280795F9F80BF CRC64;
MPFTPTDYDP YDFANRRHIG PSPAEMAEMF EVLGVKDLDE LIDQTVPKSL RQDAPLDFGA
PKSERELLWY MRQVAKKNQV FTTMIGQGFY GTVTPPAIQR NILENPAWYT AYTPYQPEIS
QGRLEALLNY QTMICDLTGL EMANASLLDE ATAAAEAMTM AQRVAKSKAT AFFVDENCHP
QNIAVMQTRA EPLGIEIVVG DPEKLDPSTV FGAIFQYPGT YGGLTDFGPH IAKLHEAGAV
GILIADPLAL CILKEPGAMG ADIAVGSTQR FGVPMGYGGP SAAYMACKDA HKRQMPGRII
GVSIDAQGGK AYRLSLQTRE QHIRREKATS NVCTAQALLA NMASFYAVFH GPEGLKAIAQ
RIHRRTARLA EVLAEAGYTV APEYFFDTLT VDVGPLQGAI LRAAREERIN LRKVGTTQVG
ISLDETTRSE TVERLCRAFG IEGAADGEAA FFRIPEGLLR ESAYLTHPVF HMNRAETEMM
RYMRRLADRD LALDRAMIPL GSCTMKLNAA AEMMPITWPE FANMHPFAPA DQAQGYADMF
RDLSEKLCVI TGYDAMSLQP NSGAQGEYAG LLTIQAYHRA RGEGHRDVCL IPTSAHGTNP
ASAQMAGMKV VVVKAAENGD IDVEDFRAKA EAAGEKLAAC MITYPSTHGV FEETVREVCE
ITHRQGGQVY IDGANMNAMV GLVRPGDLGG DVSHLNLHKT FCIPHGGGGP GMGPIGVKAH
LAPYLPGHPA TGGQEGPVSA APWGSAAILP ISWAYVLMMG GEGLTQATKV AILNANYIAK
RLEGAYGVLF NGRNGRVAHE CILDTRPFAD SAHVTVDDIA KRLIDNGFHA PTMSWPVAGT
LMVEPTESET KAELDRFVTA MLSIREEIAA IERGEMDAEN NPLKHAPHTV NALIGDWDRP
YSREQGCFPP ASFRVDKYWP PVGRVDNVYG DRHLVCICPP VESYAEAAE
//
