ID   GCSP_BRADU              Reviewed;         955 AA.
AC   Q89I86;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, 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};
GN   OrderedLocusNames=blr5753;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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; BA000040; BAC51018.1; -; Genomic_DNA.
DR   RefSeq; NP_772393.1; NC_004463.1.
DR   AlphaFoldDB; Q89I86; -.
DR   SMR; Q89I86; -.
DR   STRING; 224911.AAV28_26275; -.
DR   EnsemblBacteria; BAC51018; BAC51018; BAC51018.
DR   KEGG; bja:blr5753; -.
DR   PATRIC; fig|224911.5.peg.5868; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_5; -.
DR   InParanoid; Q89I86; -.
DR   OrthoDB; 9801272at2; -.
DR   PhylomeDB; Q89I86; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR   GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
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..955
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166907"
FT   MOD_RES         702
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   955 AA;  102392 MW;  63DF72162F811292 CRC64;
     MMTAHRKSNG DTTNFARRHI GPSARDVAAM LETVGAKSVD ALMAETLPAS IRQAAPLDLG
     KPLSETEAIA HMGELAAQNQ VFTSLIGQGY SGTILPAVIQ RNILENPAWY TAYTPYQPEI
     SQGRLEALFN FQTMICDLTG LDVANASLLD EATAAAEAMA LAERHSRVEA KAFFVDKDVH
     PQTLAVMRTR AEPLGWNLIV GDPLTDLDKA DVLGALLQYP GSSGALRDLR PAIAALKAKG
     ALAIVAADLL ALTLLASPGE LGADIAIGSA QRFGVPMGYG GPHAAYMAVR DALKRSLPGR
     IVGLSVDSRG MPAYRLALQT REQHIRREKA TSNICTAQVL LAVIAAMYAV YHGPEGLSQI
     ARQVHRRAAV LAAGLRKLGF APHSDSFFDT LSVDAGAKRA EIVARAAAEK INLGVGETAL
     RIALDETTTP ATVEAVWRAF GGQLAYAELD ATTREALPEA LKRTTAFLTH PVFHAHRSET
     EMLRYMRKLS DRDLALDRAM IPLGSCTMKL NATTEMMPLT WPEFGSLHPF APREQAKGYH
     ALFARLEKWL CDITGYDAIS LQPNSGAQGE YAGLLAIRGY HAARGEAHRK ICLIPSSAHG
     TNPASAAMVG MDVVVVACEK NGDVDVNDLR AKADKHANDL AAIMITYPST HGVFEEHIRE
     ICDIVHGHGG QVYLDGANLN AQVGLSRPGD YGADVSHLNL HKTFCIPHGG GGPGMGPIGV
     KAHLAPFLPG HPATRGDAPV GPVSAAPFGS ASILTISYIY ILMMGGEGLK RATEIAILNA
     NYIAARLDAH FPVLYKNARG RVAHECIVDP RALKTTSGVT VDDIAKRLID YGFHAPTMSF
     PVPGTLMIEP TESESKAELD RFCDAMIAIR KEIGEVEAGR FKIEASPLRH APHTVHDIAD
     DAWARAYSRA EGCFPDGVSR TDKYWSPVGR VDNVYGDRNL VCSCPPVSDY AEAAE
//