ID   GCSP_SODGM              Reviewed;         953 AA.
AC   Q2NRF0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=SG2000;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=morsitans;
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA   Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights into
RT   the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL   Genome Res. 16:149-156(2006).
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; AP008232; BAE75275.1; -; Genomic_DNA.
DR   RefSeq; WP_011411730.1; NZ_LN854557.1.
DR   AlphaFoldDB; Q2NRF0; -.
DR   SMR; Q2NRF0; -.
DR   STRING; 343509.SG2000; -.
DR   EnsemblBacteria; BAE75275; BAE75275; SG2000.
DR   KEGG; sgl:SG2000; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000001932; 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..953
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045621"
FT   MOD_RES         705
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   953 AA;  103555 MW;  836B7A91EA51DFA2 CRC64;
     MTQTLSQLEH HDAFIARHIG PSAPQQVHML ATVGSDSLAG LIAQIVPADI QLAAAPAVGE
     ATTEAQALAE LKAIARQNQR YKSFIGMGYS AVVTPPVILR NMLENPGWYT AYTPYQPEVS
     QGRLEALLNF QQLTLDLTGL DIASASLLDE ATAAAEAMAL AKRSSKLKQA NCFFVADDVH
     PQTLDVLRTR AGTFGFELVI DKAQAALEHP DLFGVLLQQV GTTGELHDYR ALMAELTRRK
     IISCVAADML SLVLLAAPGE QGADVVFGSS QRFGVPMGYG GPHAAFFAAR DEMKRAMPGR
     IIGVSRDAAG DTALRMVMQT REQHIRREKA NSNICTSQVL LANIAGLYAV YHGPQGLKRI
     AGRIHRLTTI LAQGLHDADL TLRHDRWFDT LTVEVVDKAG VLARANAAGI NLRSDIHGAV
     GITLDETTVR EDVQTLWQVV TGAAGTLAID ALDAGCDEVI PPELLRATPI LTHEVFNRYH
     SETEMMRYMH RLERKDLALN QAMIPLGSCT MKLNAAAEMI PITWPEFAEL HPFCPPEQAA
     GYQQMIAQLS RWLIQLTGYD ALCMQPNSGA QGEYAGLLAI RRYHESRNQG ERHICLIPSS
     AHGTNPASAQ MAGMSVTVVA CDKNGNIDLH DLRAKAEQAG EQLSCIMVTY PSTHGVYEET
     IREVCQIVHQ YGGQVYLDGA NMNAQVGITS PGYIGADVSH LNLHKTFCIP HGGGGPGMGP
     IGVKAHLAPF VPGHLVVELD GVLTRQGAVS AAPFGSASIL PISWMYIRMM GAEGLKQASQ
     VAILNANYIA TRLQQAYPVL YTGRAGRVAH ECILDIRPLK EATGISEMDI AKRLIDYGFH
     APTMSFPVAG TLMVEPTESE SQLELDRFID AMLAIRAEIQ QVADGVWPAS DNPLVNAPYT
     QRELAGEWRH PYDRQIAAFP AGYGDKYWPA VKRLDDVYGD RNLFCACVPL SDY