ID   GCSP_RHILO              Reviewed;         937 AA.
AC   Q98LT6;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=mlr0885;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000012; BAB48377.1; -; Genomic_DNA.
DR   RefSeq; WP_010909731.1; NC_002678.2.
DR   AlphaFoldDB; Q98LT6; -.
DR   SMR; Q98LT6; -.
DR   STRING; 266835.14021766; -.
DR   PRIDE; Q98LT6; -.
DR   EnsemblBacteria; BAB48377; BAB48377; BAB48377.
DR   KEGG; mlo:mlr0885; -.
DR   PATRIC; fig|266835.9.peg.704; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_5; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000000552; 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..937
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166931"
FT   MOD_RES         686
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   937 AA;  99386 MW;  D135C7B4C9DD0471 CRC64;
     MMTTALTPFS ARHIGPGVND VRAMLAVIGV PSVETLISQA VPQSIRLDLP LTLPAPASEA
     EALAELSAIM AKNTVLKSFI GAGYHGVHVP PVIQRNLFEN PAWYTAYTPY QAEISQGRLE
     MLFNFQTLVT ELTGLPVASA SLLDEATAVA EAVGIALRHH RDKRTKVAFA GTPHPQTLDV
     VRTRAEPLGI EIDGETIDDN TAALLVSWPD TLGVYGDHKA AIDKARAAGA LVVFIADPLG
     LTLTDAPAKL GADIAVGPMQ RFGVPMGFGG PHAAYCAVSD RLTRLMPGRL VGQSTDSKGR
     PGYRLALQTR EQHIRRDKAT SNICTAQALL ANMATAYAIW HGPAGLQAIA GRIHALANRL
     ASGLKAAGVS VLGASRFDTV TVEAKGKAAE IAEAAEKTGR LLRVLDADHV GIAFDETSTD
     ADLDAIASLF GAKAAPSADS TVPGKPRGKE FLTQPVFNEN KSETDMMRLL RRLADKDLAL
     DRSMIPLGSC TMKLNAAAEM MPVSWPSIAD LHPFAPASHS AGYRAMIGEL EGWLSEITGF
     DAVSLQPNAG SQGEYAGLLA IRAYHRSRGE GHRTVCLIPS SAHGTNPASA AMAGMSVVVV
     RCLEDGNIDM DDMRAKANEH SKNLAALMFT YPSTHGVYEE GARHLCALIH EHGGQVYFDG
     ANLNALVALA RPADIGADVC HMNLHKTFCI PHGGGGPGVG PIGVKAHLKP YLPGHVTEGS
     AHAVSAAPFG SASILPITWM YIRMMGAAGL KQATETAIIS ANYVATRLAP HFPLLYKGRH
     DRIAHECILD TRVLKESAGI SVDDIAKRLI DYGFHAPTMS FPVAGTLMVE PTESEPKREL
     DRFCEAMIAI AGEAAKVARG DWPLADNPLV NAPHTAAETL AGQWTHPYSR LEAAYPAGDA
     DTAAKYWPPV SRIDNVAGDR NLVCSCPPLS DYLGAAE