ID GCSP_SACD2 Reviewed; 964 AA.
AC Q21HU3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000255|HAMAP-Rule:MF_00711};
DE EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine cleavage system P-protein {ECO:0000255|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine decarboxylase {ECO:0000255|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000255|HAMAP-Rule:MF_00711};
GN Name=gcvP {ECO:0000255|HAMAP-Rule:MF_00711}; OrderedLocusNames=Sde_2476;
OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Saccharophagus.
OX NCBI_TaxID=203122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2-40 / ATCC 43961 / DSM 17024;
RX PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M.,
RA Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA Richardson P.M., Borovok I., Hutcheson S.;
RT "Complete genome sequence of the complex carbohydrate-degrading marine
RT bacterium, Saccharophagus degradans strain 2-40 T.";
RL PLoS Genet. 4:E1000087-E1000087(2008).
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:0000255|HAMAP-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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00711};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00711};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000255|HAMAP-Rule:MF_00711}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000255|HAMAP-
CC Rule:MF_00711}.
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DR EMBL; CP000282; ABD81736.1; -; Genomic_DNA.
DR RefSeq; WP_011468953.1; NC_007912.1.
DR AlphaFoldDB; Q21HU3; -.
DR SMR; Q21HU3; -.
DR STRING; 203122.Sde_2476; -.
DR KEGG; sde:Sde_2476; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_1_1_6; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000001947; 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:SF13; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 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; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..964
FT /note="Glycine dehydrogenase (decarboxylating)"
FT /id="PRO_1000045605"
FT MOD_RES 710
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ SEQUENCE 964 AA; 105798 MW; FB71E12D9684E34A CRC64;
MSHGTSLDEL FNSRDFIGRH IGPNADQTRA MLDAMGLDSI DQLIDLTVPA SIRGEETRAL
AAPVNEQQAL AELKNIAGNN QRFKSYIGMG YHPTYVPPVI LRNVLENPGW YTAYTPYQPE
IAQGRLEGLL NFQQMIIELT GMDMANASML DEATAAAEAM AMAKRVARKN KSNTFFADKH
CHPQTLAVLQ TRASHFGFEL VIGDITQDLN KQEVFGAITQ YPGTSGEVKD LRPIVNQAHE
QDALLIVAAD ILSLVLLESP GAMGADIVVG SNQRFGIPMG FGGPHAAFFG FREKYKRATP
GRIIGVSVDT RGKRALRMAM QTREQHIRRE KANSNICTSQ VLLAVMSVFY AMYHGSAGVT
RIAQRVHTLT KMLAQGLTAQ GHKLAFDNYF DTLCVIVNDQ QQGLFDRAQQ AGVNLRKLDK
NALTISLNEC TSLEDIHQLL DIFSLGKHSQ DVKSLETKAL AAEVIPASCR REGPALNHPV
FEQYHSETEM LRYLKRLESK DIALNHAMIP LGSCTMKLNA TAEMIPVTWP EFGELHPFAP
MEQAAGYSTL FTQLQDMLKA CTGYDAISLQ PNAGSQGEYA GLVAIRKYFE HLGQTERNIC
LIPASAHGTN PASAQMVEMK VVVVACDNLG NVDLNDLKAK VAQYGETIAA LMVTYPSTHG
VFEEEITAIC DLIHSVGAQV YIDGANMNAL VGLAAPGKFG GDVSHLNLHK TFCIPHGGGG
PGMGPIGVKS HLAPFLAGHP VQPVPNTLVE NGTISAAPWG SASILTISWM YIRMMGAEGM
KRATEFAILN ANYIAHRLQD HYPILYKGKN GYIAHECLLD LRPLKESSGI TEEDIAKRLM
DFGFHAPTMS FPVAGTLMIE PTESESQAEL DRFCDAMIKI RQEASLVESG ELPRDNNPLV
NAPHTLDDAL DETWTRPYTR DEATRPLPYL HAHKIWPTVN RIDNVYGDRN LICSCPSIES
YTEE
//
