ID   GCSP_BRASB              Reviewed;         957 AA.
AC   A5EMM2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=BBta_5451;
OS   Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX   NCBI_TaxID=288000;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTAi1 / ATCC BAA-1182;
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(2007).
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; CP000494; ABQ37416.1; -; Genomic_DNA.
DR   RefSeq; WP_012045378.1; NC_009485.1.
DR   AlphaFoldDB; A5EMM2; -.
DR   SMR; A5EMM2; -.
DR   STRING; 288000.BBta_5451; -.
DR   EnsemblBacteria; ABQ37416; ABQ37416; BBta_5451.
DR   KEGG; bbt:BBta_5451; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_5; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000000246; 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.
FT   CHAIN           1..957
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000062072"
FT   MOD_RES         702
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   957 AA;  102983 MW;  CCCF1AE158731F2A CRC64;
     MTTPLKPLDD AATSFARRHI GPSPRDVAAM LETVGAKSVA ELMAQTLPGT IRQATPLTLE
     PALSEVEAIG HMRALAAQNQ VFTSLIGQGY SGTIMPAVIQ RNILENPAWY TAYTPYQPEI
     SQGRLEALFN FQTMICDLTG LDVANASLLD EGTAAAEAMA LAERSARAKT KAFFVDRNVH
     PQTLAVLRTR AEPLGWQLIV GDPVKDLDGA EVFGGLLQYP ETTGALRDPR ADIAKLHDKG
     ALAILAADLL ALTVIASPGE LGADIAIGSA QRFGVPMGYG GPHAAYMAVR DALKRSLPGR
     IVGLSVDSRG APAYRLALQT REQHIRREKA TSNICTAQVL LAVIAAMYAV YHGPDGLKSI
     ARTVHRRAAV LAAGLRKLGF APASDSFFDT VLVEAGANCD EIIARAESQR INLGRDGSRL
     RIALDETTTA DVVEAVWRAF GGELSYAAIE AEARDAVPAE LKRQRPFLTH PVFHAHRSET
     EMLRYLRKLA DRDLALDRAM IPLGSCTMKL NATTEMIPLT WPEFSSLHPF VPRAQAAGYH
     TMFADLQDWL CRISGYDAVS LQPNSGAQGE YAGLLAIRGY HAARGEGHRT ICLIPSSAHG
     TNPASAHMVG MEVVVVGCDS NGNVDLADLK AKAELHSAKL AAIMITYPST HGVFEEHIRD
     ICDIVHAHGG QVYLDGANLN AQVGLSRPGD YGADVSHFNL HKTFCIPHGG GGPGMGPIGV
     KAHLAPFLPG HPATDAATPS PVGPVSAAPY GSASILTISY IYMLLMGGEG LTRATEIAIL
     NANYVAARLD PHFPVLYRNE RGRVAHECII DPRPLKQTCG VTVDDIAKRL IDYGFHAPTM
     SFPVAGTLMI EPTESESKAE LDRFCDAMIA IRKEIAAVEQ GRFTIEASPL RHAPHTVHDI
     ADDDWNRVYR RSEGCFPEGT SRTDKYWCPV GRVDNVYGDR NLVCSCPPIG DYAQAAE