ID   GCSP_RHIEC              Reviewed;         954 AA.
AC   Q2K813;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 117.
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=RHE_CH02243;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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; CP000133; ABC91023.1; -; Genomic_DNA.
DR   RefSeq; WP_011425504.1; NC_007761.1.
DR   AlphaFoldDB; Q2K813; -.
DR   SMR; Q2K813; -.
DR   KEGG; ret:RHE_CH02243; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_4_0_5; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000001936; 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: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; Reference proteome.
FT   CHAIN           1..954
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045599"
FT   MOD_RES         704
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   954 AA;  104034 MW;  50338D5932DA1EC8 CRC64;
     MTTPTEFQFT DYQPYDFANR RHIGPSPAEM AEMLKVIGYN SLEGLIDATL PPAIRQKAPL
     VWGAPMTERE ALDKLRETAN KNKVLVSLIG QGYYGTITPP VIQRNILENP AWYTAYTPYQ
     PEISQGRLEA LLNYQTMVCD LTGLDIANAS LLDEATAAAE GMAMAERVAK SKAKAFFVDA
     DCHPQTIALI RTRAEPLGWS VIVGNPFTDL DPVDVFGAIF QYPGTHGHVH DFTGLIARLH
     QAGAISVVAA DILALTLLKS PGEMGADIAV GSSQRFGVPV GYGGPHAAFM AVRDAIKRAM
     PGRLVGVSVD ARGNRAYRLS LQTREQHIRR EKATSNICTA QVLLAVMASM YAVFHGPDGI
     KAIAQQVHQK AVLMAKGLEK LGYKVEPESF FDTITVDVGH MQGLILRAAV AEGVNLRKVG
     ETKIGMSLDE RTRPATLEAV WRAFGGNFTI ADFEPSYRLP KALLRTSEYL SHPIFHMNRA
     ESEMTRYIRR LSDRDLALDR AMIPLGSCTM KLNATAEMLP ITWPEFSDIH PFVPADQALG
     YREMLDDLTE KLCAVTGYDA FSMQPNSGAQ GEYAGLLTIR NYHIANGEGH RDVCLIPTSA
     HGTNPASAQM VGMKVVVVKV RENGDIDMED FRAKAEEHAA NLSCCMITYP STHGVFEETV
     KEICELVHKH GGQVYLDGAN MNAMVGLSRP GDIGSDVSHL NLHKTFCIPH GGGGPGMGPI
     GVKAHLAPHL PGHPETDGRP GAVSAAPFGS ASILPISWSY CLMMGGEGLT QATKVAILNA
     NYIATRLKGA YNVLYKSKTG RVAHECIIDT RPLVDSSGVT VDDVAKRLID CGFHAPTMSW
     PVAGTLMIEP TESETKAELD RFCEAMLAIR EEARAIEDGR MDKTNNPLKN APHTVEDLVG
     EWDRPYSREQ ACFPPGAFRV DKYWSPVNRV DNVYGDRNLI CTCPPVESYA EAAE
//