ID   GCSP_MYCLB              Reviewed;         952 AA.
AC   B8ZSN5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=MLBr02072;
OS   Mycobacterium leprae (strain Br4923).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=561304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Br4923;
RX   PubMed=19881526; DOI=10.1038/ng.477;
RA   Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A.,
RA   Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C.,
RA   Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H.,
RA   Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R.,
RA   Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A.,
RA   Rougemont J., Brennan P.J., Cole S.T.;
RT   "Comparative genomic and phylogeographic analysis of Mycobacterium
RT   leprae.";
RL   Nat. Genet. 41:1282-1289(2009).
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; FM211192; CAR72169.1; -; Genomic_DNA.
DR   RefSeq; WP_010908701.1; NC_011896.1.
DR   AlphaFoldDB; B8ZSN5; -.
DR   SMR; B8ZSN5; -.
DR   EnsemblBacteria; CAR72169; CAR72169; MLBr02072.
DR   KEGG; mlb:MLBr02072; -.
DR   HOGENOM; CLU_004620_3_2_11; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000006900; Chromosome.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProt.
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..952
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000147967"
FT   MOD_RES         703
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   952 AA;  101283 MW;  ADC68B6265C3D8FF CRC64;
     MSVPNSSNKQ TCFTARHIGP NSEDVATMLA VIGVESLDDL AAKAVPSDIL DNVTDTGVAP
     GLDRLPPPAT ESETLAELGA LARANTVAVS MIGQGYYDTL TPAVLSRNIL ENPAWYTPYT
     PYQPEISQGR LEALLNFQTL VSDLTGLEIA NASMLDEGTA AAEAMTLMYR AARSTASRVV
     VDVDVFAQTV AVFATRAKPL GIDIVVADLR EGLPDGEFFG VITQLPGASG RITDWTALIA
     QAHSRGALVA VGADLLALTL ITPPGEIGAD VAFGTTQRFG VPMGFGGPHA GYLALHTKHA
     RQLPGRLVGV SVDSDGTPAY RLALQTREQH IRRDKATSNI CTAQVLLAVM AAMYASYHGA
     EGLTGIARRV HAQARALAAG LSAAGVEVVH QAFFDTVLAR VPGRTVQIQG AAKERGINVW
     LVDGDHVSVA CDEATTDEHI TAVLAAFAAT PARASFAGPD IATRTSAFLT HPTFTKYRTE
     TSMMRYLRAL ADKDIALDRS MIPLGSCTMK LNAAAEMESI TWQEFTRQHP FAPVSDTPGL
     RRLISDLESW LVQITGYDAV SLQPNAGSQG EYAGLLAIHD YHVSRGEPHR NVCLIPSSAH
     GTNAASAALV GMRVVVVGCH DNGDVDLDDL RIKLSEHANR LSVLMITYPS THGVYEHDIA
     EICAAVHDAG GQVYVDGANL NALVGLARPG KFGGDVSHLN LHKTFCIPHG GGGPGVGPVA
     VRSHLVSFLP GHPFAPELPQ GQPVSSAPYG SASLLPITWA YIRMMGADGL RTASLTAIAS
     ANYIARRLDK YFPVLYTGEN GMVAHECILD LRPITKSVGV TVDDVAKRLA DYGFHAPTMS
     FPVPGTLMVE PTESESLAEI DAFCEAMIAI RGEIARVGAG EWSVEDNPLR GAPHTAECLL
     ASDWDHPYTR EEAAYPLGKA FRPKVWPPVR RIDGVYGDRN LVCSCLPVEA FV