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   25-MAY-2022, entry version 96.
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; Proteobacteria; 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=(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] +
CC         glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-
CC         [glycine-cleavage complex H protein] + CO2; 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   EnsemblBacteria; ABD81736; ABD81736; Sde_2476.
DR   KEGG; sde:Sde_2476; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
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; 3.40.640.10; -; 2.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR003437; GcvP.
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   PANTHER; PTHR11773; PTHR11773; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; SSF53383; 2.
DR   TIGRFAMs; TIGR00461; gcvP; 1.
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