ID   GCSP_VARPS              Reviewed;         968 AA.
AC   C5CRW8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
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};
GN   OrderedLocusNames=Vapar_3301;
OS   Variovorax paradoxus (strain S110).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=543728;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S110;
RX   PubMed=21183664; DOI=10.1128/jb.00925-10;
RA   Han J.I., Choi H.K., Lee S.W., Orwin P.M., Kim J., Laroe S.L., Kim T.G.,
RA   O'Neil J., Leadbetter J.R., Lee S.Y., Hur C.G., Spain J.C.,
RA   Ovchinnikova G., Goodwin L., Han C.;
RT   "Complete genome sequence of the metabolically versatile plant growth-
RT   promoting endophyte, Variovorax paradoxus S110.";
RL   J. Bacteriol. 193:1183-1190(2011).
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; CP001635; ACS19919.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5CRW8; -.
DR   SMR; C5CRW8; -.
DR   STRING; 543728.Vapar_3301; -.
DR   KEGG; vap:Vapar_3301; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_4; -.
DR   OrthoDB; 9801272at2; -.
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; Pyridoxal phosphate.
FT   CHAIN           1..968
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000212658"
FT   MOD_RES         713
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   968 AA;  104204 MW;  8DFF68ABC656715D CRC64;
     MPIPALPSLQ QLENAEEFLA RHIGIDAADE ARMLPVIGSE TRAELIDGIV PAAIRRAKPM
     RLPAPATEAD ALAELKAIAA KNKVFRSFIG QGYYGTHTPG VILRNVLENP AWYTAYTPYQ
     AEISQGRMEA LLNFQTMVCD LTGMAIANAS MLDEATAAAE AMTLAKRSVK SKSNVFLVSG
     DCHPQTIEVI KTRAAPLGIE VKVSTVSETL PHLMVSGEFF GVLAQYPATT GHVHDLRPLA
     GHAHQCDAAF CVAADLLALT LLAPPGEWDA DIVCGTTQRF GMPMCNGGPH AAYLACRDEF
     KRSLPGRLVG VSVDTHGQPA YRLALQTREQ HIRREKATSN ICTAQVLPAV VASMYAVYHG
     PDGLTRIAQR VAALTAILAQ GLAQMGREPV NGTAFDSLTI RTGDDTPKII ERAQAAGVNL
     RQRLQQHLGI SLDETTTRAD IETLWALFVP AGTPMPRFDD LANAVPRLPE DLRRTSAFLT
     HPVFNTHKSE TAMLRYIRSL SDKDLALDRS MIPLGSCTMK LNATSEMIPI TWPEFANIHP
     FAPAEQLVGY AQLDAQLRAW LCEATGYAGI SLQPNAGSQG EYAGLLAIRS FHEANGQGHR
     NICLIPSSAH GTNPASAQMV GLQVVVTACD AQGNVDMDDL RRACEKHSDK LAAVMITYPS
     THGVFETRVK ELCELVHEHG GRVYVDGANM NALVGVAAPG EFGGDVSHLN LHKTFCIPHG
     GGGPGVGPVC VVEDLVPYLP GHATAGVASN GVGAVSAAPL GNAAVLPISW MYCRMMGAKG
     LQAATEIAIL SANYISARLK DHYPTLYASP NGHVAHECIL DLRPLKDSSG VTAEDVAKRL
     IDYGFHAPTL SFPVPGTLMV EPTESEPLAE LDRFIDAMIA IRGEIRRVEE GVWPKDDNPL
     KHAPHTAASL MAAEWPHPYS RELGAFPLAE LKLAKYWPPI GRVDNVYGDR NLFCSCVPVG
     DYKETEEA
//