ID   GCSP_SINMW              Reviewed;         954 AA.
AC   A6U8Q3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 80.
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=Smed_1182;
OS   Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=366394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA   Richardson P.;
RT   "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000738; ABR60033.1; -; Genomic_DNA.
DR   RefSeq; WP_011975351.1; NC_009636.1.
DR   RefSeq; YP_001326868.1; NC_009636.1.
DR   AlphaFoldDB; A6U8Q3; -.
DR   SMR; A6U8Q3; -.
DR   STRING; 366394.Smed_1182; -.
DR   PRIDE; A6U8Q3; -.
DR   EnsemblBacteria; ABR60033; ABR60033; Smed_1182.
DR   GeneID; 61612037; -.
DR   KEGG; smd:Smed_1182; -.
DR   PATRIC; fig|366394.8.peg.4310; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_4_0_5; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000001108; 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..954
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045620"
FT   MOD_RES         704
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   954 AA;  104061 MW;  9A09A8613FE27986 CRC64;
     MSMPKDFTFT DYKPYDFANR RHIGPSPAEM DEMLKVVGYP SLDALIDDTV PPSIRQQTPL
     AWGAPMTERE ALDKLRETAN RNRKVVSLIG QGYYGTITPP VIQRNILENP AWYTAYTPYQ
     PEISQGRLEA LLNFQTMVCD LTGLDVANAS LLDEATAAAE AMAIAERVAK SKAKAFFVDE
     NCHPQTIALL KTRAEPLGWQ IVVGNPFEDL DAAIVFGAIF QYPGTYGHVR DFSGLIARLH
     ELGAIAAVAA DPLALALLKS PGEMGADIAV GSTQRFGVPV GYGGPHAAYM AVRDAYKRSM
     PGRLVGVSVD ARGNRAYRLS LQTREQHIRR EKATSNICTA QVLLAVMASM YAVFHGPEGI
     KAIAQSVHQK TVRLALGLEK LGYTVEPDVF FDTITVEVGK LQGIILKAAV AEDVNLRKIG
     TTKIGISLDE RSRPITLEAV WRAFGGDFSV DQFEPDYRLP KELLRTSDYL THPIFHMNRA
     ESEMTRYMRR LADRDLALDR AMIPLGSCTM KLNATAEMLP ITWPEFSEIH PFVPADQAMG
     YHHLIEDLSQ KLCAITGYDA ISMQPNSGAQ GEYAGLLAIR AYHIANGNEH RDVCLIPTSA
     HGTNPASAQM AGMKVVVVKV SDAGEIAMDD FRAKAEQYAE TLSCCMITYP STHGVFEENV
     REVCEIVHKH GGQVYLDGAN MNAMVGLSRP GDIGSDVSHL NLHKTFCIPH GGGGPGMGPI
     GVKAHLAPFL PGHPESGEHK GAVSAAPFGS ASILPISWSY CLMMGGEGLT QATKVAILNA
     NYVAARLKGA FDVLYKSAKG RVAHECIIDT RPLAESAGVT VDDVAKRLID CGFHAPTMSW
     PVAGTLMIEP TESETKAELD RFCDALLAIR EEARAIAEGR MDKINNPLKN APHTVEDLVG
     DWDRPYSREQ ACFPPGAFRV DKYWSPVNRV DNVYGDRNLV CTCPPIESYA EAAE