ID A0A3D8VBF8_9GAMM Unreviewed; 963 AA.
AC A0A3D8VBF8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-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:RDY66589.1};
GN ORFNames=DX912_12640 {ECO:0000313|EMBL:RDY66589.1};
OS Lysobacter soli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=453783 {ECO:0000313|EMBL:RDY66589.1, ECO:0000313|Proteomes:UP000256829};
RN [1] {ECO:0000313|EMBL:RDY66589.1, ECO:0000313|Proteomes:UP000256829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 22011 {ECO:0000313|EMBL:RDY66589.1,
RC ECO:0000313|Proteomes:UP000256829};
RA Zhang X., Feng G., Zhu H.;
RT "Lysobacter soli KCTC 22011, whole genome shotgun sequence.";
RL Submitted (AUG-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:RDY66589.1}.
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DR EMBL; QTJR01000008; RDY66589.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8VBF8; -.
DR Proteomes; UP000256829; 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:UP000256829}.
FT DOMAIN 18..438
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 442..741
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 778..899
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 701
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 963 AA; 103930 MW; B6D1DBB5218402CF CRC64;
MSQKTSLRAL EHHDAFLERH IGPNDAEIAQ MLGVVGFDSL DAMTDAIVPA SIKSPKPLDL
PAPITEVEAI AKIRAIADRN QVFKSFIGQG YYGTHTPNVI LRNILENPAW YTAYTPYQAE
ISQGRMEALI NFQTMCAELT GMEIANASLL DEATAAAEAM TLAKRSAKSK SNTFFVSSGV
HPQTLEVLRT RAEPLEIELV VADDSEAASI DSFGVLLQYP NTFGQIHDYK ALADAVHARG
GLVAVATDLL ALTLIAAPGE WGADIVVGNT QRFGVPFGFG GPHAAFMACR DAYKRSMPGR
LIGVSIDAEG KAAYRLTLQT REQHIRREKA TSNICTAQVL LAVMASMYAV YHGPDGLQRI
ARRTHRLASI LATALRNAGI TVGPDFFDTL HVVDVDAGAI HAKAVEARIN LRRIDGRSLG
ISLDETTTRA DVVALAALFG AKIDVDALDA TVDDALPNGL LRTSAFLTHP VFNTHHSEHE
LLRYMRSLAD KDLAMDRTMI PLGSCTMKLN ATAEMIPVTW PEFGNLHPLA PGAQAAGYQQ
LIGELEAMLV ECTGYDAVSL QPNSGAQGEY AGLLAIRAYH RSRGEAHRDI CLIPDSAHGT
NPASAQMCGM QVVVTKTDGN GNVDVEDIRR NAEKYSDRLA AIMMTYPSTH GVFEEEVVEI
CEIIHKHGGQ VYTDGANMNA LVGVAKPGKW GSDVSHLNLH KTFCIPHGGG GPGVGPCAVK
SHLAPFLPGA LNADGVKTDG VGNGDVGMVS AASFGSASIL PISWMYVTMM GAAGLRRATQ
VALLNANYIA RRLAPHYETL YTGRNDLVAH ECILDLRPLK DSTGVSAEDV AKRLIDFGFH
APTLSFPVAG TLMVEPTESE SLHELDRFID AMIQIRDEIR AVEEGKLDRE DNPLKNAPHT
ATAVSASEWT HAYPRELAAF PLPSLRLQKY WPPVARVDNV YGDKNVMCAC IPVDAYKDDE
VEA
//
