ID   GCSP_BRASO              Reviewed;         957 AA.
AC   A4YXQ9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=BRADO4984;
OS   Bradyrhizobium sp. (strain ORS 278).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX   NCBI_TaxID=114615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ORS 278;
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; CU234118; CAL78685.1; -; Genomic_DNA.
DR   RefSeq; WP_012028626.1; NC_009445.1.
DR   AlphaFoldDB; A4YXQ9; -.
DR   SMR; A4YXQ9; -.
DR   STRING; 114615.BRADO4984; -.
DR   EnsemblBacteria; CAL78685; CAL78685; BRADO4984.
DR   KEGG; bra:BRADO4984; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_4_1_5; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   BioCyc; BSP114615:BRADO_RS23160-MON; -.
DR   Proteomes; UP000001994; 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..957
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000062073"
FT   MOD_RES         702
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   957 AA;  102667 MW;  B875D6C70B7C1F3A CRC64;
     MTTPLKPLDD AATSFARRHI GPSPRDVAAM LETVNAKSVA ELMAQTLPGT IRQAAPLDIG
     PALSETEALS HMRALAAQNQ VFTSLIGQGY AGTIMPAVIQ RNILENPAWY TAYTPYQPEI
     SQGRLEALFN FQTMICDLTG LDVANASLLD EGTAAAEAMA LAERSARAKT KAFFVDHNVH
     PQTLTVLRTR AEPLGWKLIV GDPAGDLDGA EVFGGLLQYP DTTGALRDPR AAIAKLHDKG
     ALAILAADLL ALTLIASPGE LGADIAIGSA QRFGVPMGYG GPHAAYMAVR DALKRSLPGR
     IVGLSVDSRG APAYRLALQT REQHIRREKA TSNICTAQVL LAVIAAMYAV YHGPAGLKAI
     ARTVHRRTAV LAAGLRKLGF APANDAFFDT VTVEAGANAS SIIARAEAER INLGHNGSRL
     RIALDETTTA DVVEAAWRAF GGELSYADIE AEARDAVPAE LKRQRPYLTH PVFHAHRSET
     EMLRYLRKLA DRDLALDRAM IPLGSCTMKL NATTEMIPLT WPEFSSLHPF VPRAQAAGYH
     AMFADLQDWL CRISGYDAVS LQPNSGAQGE YAGLLAIRGY HAARGEAHRT ICLIPSSAHG
     TNPASAHMVG MEVVVVGCDA GGNVDLADLK AKAEAHSQKL AAIMITYPST HGVFEEHIRD
     ICDIVHAHGG QVYLDGANLN AQVGLARPGD YGADVSHFNL HKTFCIPHGG GGPGMGPIGV
     KAHLAPFLPG HPATDGKTAH PVGPVSAAPY GSASILTISY IYMLLMGGEG LTRATEIAIL
     NANYVAARLD AHFPVLYRNE RGRIAHECII DPRLLKQTSG VTVDDIAKRL IDYGFHAPTM
     SFPVAGTLMI EPTESESKAE LDRFCDAMIA IRKEIAEVEQ GRFTIEASPL RHAPHTVHDI
     ADDEWSRAYR RSEGCFPAGS SRTDKYWCPV GRVDNVYGDR NLVCSCPPVE DYAQAAE