GCSP_RHIEC
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 25-MAY-2022, entry version 110.
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=RHE_CH02243;
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Proteobacteria; 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=(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; CP000133; ABC91023.1; -; Genomic_DNA.
DR RefSeq; WP_011425504.1; NC_007761.1.
DR AlphaFoldDB; Q2K813; -.
DR SMR; Q2K813; -.
DR STRING; 347834.RHE_CH02243; -.
DR EnsemblBacteria; ABC91023; ABC91023; RHE_CH02243.
DR KEGG; ret:RHE_CH02243; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_4_0_5; -.
DR OMA; CVPMSEY; -.
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; 3.40.640.10; -; 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..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