ID A0A2T4JI52_9RHOB Unreviewed; 946 AA.
AC A0A2T4JI52;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:PTE17586.1};
GN ORFNames=C5F46_08690 {ECO:0000313|EMBL:PTE17586.1};
OS Phaeovulum veldkampii DSM 11550.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Phaeovulum.
OX NCBI_TaxID=1185920 {ECO:0000313|EMBL:PTE17586.1, ECO:0000313|Proteomes:UP000241899};
RN [1] {ECO:0000313|EMBL:PTE17586.1, ECO:0000313|Proteomes:UP000241899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11550 {ECO:0000313|EMBL:PTE17586.1,
RC ECO:0000313|Proteomes:UP000241899};
RA Meyer T.E., Miller S., Lodha T., Gandham S., Chintalapati S.,
RA Chintalapati V.R.;
RT "Rhodobacter veldkampii.";
RL Submitted (MAR-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:PTE17586.1}.
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DR EMBL; PZKF01000016; PTE17586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4JI52; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000241899; 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:UP000241899}.
FT DOMAIN 16..438
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 469..727
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 765..885
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 697
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 946 AA; 101572 MW; 9B9B344902878875 CRC64;
MTFTPTAYDS YDFANRRHIG PSPVEMAEML QAVGAPSLDA LIEETVPGSI RQTTALSWEP
LTEHAALEKM RAVAAKNRVM VSLIGQGYYG CVTPPAIQRN ILENPAWYTA YTPYQPEIAQ
GRLEALLNYQ TMVCDLTGLP VANASLLDEA TAAAEAMAMA ERVAKSKARV FFVDENCHPQ
TIGVIRTRAQ PLGIEVLVGA PDALEPGMVF GAIFQYPGTY GHVRDFTAEI EALHAAKAVA
IVACDLLALC LLKEPGAMGA DIAIGSAQRF GVPMGYGGPH AAFMSCRDEF KRAMPGRIVG
VSIDARGGRA YRLSLQTREQ HIRREKATSN VCTAQALLAV MASFYAVFHG PRGLRAIAER
VHFTAQSLAN ALKDAGAKVR PGAFFDTITV EVGVGQAGIL AAAEQRGINL RKVGRDRVGI
SVDETTTPAI VARLLDAFGI HDPVQPVSGL GFPEGLLRQS DYLTHPVFHM NRAESEMMRY
MRRLSDRDLA LDRAMIPLGS CTMKLNAAAE MMPISWPGFS SLHPFAPAHQ AQGYAEAIED
LTSKLCEITG YDAFSMQPNS GAQGEYAGLL TIAAWHRARG EEHRDICLIP VSAHGTNPAS
AQMAGMQVVV VKSAPNGDID IEDFAAKAKA AGDRLAACMI TYPSTHGVFE ETVRRVCELT
HAYGGQVYLD GANMNALVGL AKPGEIGSDV SHLNLHKTFA IPHGGGGPGM GPIGVKAHLA
PYLPGHPVTG GTEGPVSAAP FGSASILLIS WAYCLMMGGE GLTQATKVAI LNANYIAARL
RGAYPILFMG NRGRVAHECI LDTRPFADHG VTVDDIAKRL IDNGFHAPTM SWPVPGTLMV
EPTESETKAE LDRFITALLA IRAEIDDVAE GRITAEASPL RHAPHTVEDL VADWDRAYSR
EQGCFPPGAF RVDKYWPPVG RVDNVYGDRN LICTCPPIEA YAEAAE
//
