ID   GCSP_MYCTA              Reviewed;         941 AA.
AC   A5U3J9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=MRA_1843;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
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; CP000611; ABQ73599.1; -; Genomic_DNA.
DR   RefSeq; WP_003900418.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U3J9; -.
DR   SMR; A5U3J9; -.
DR   STRING; 419947.MRA_1843; -.
DR   EnsemblBacteria; ABQ73599; ABQ73599; MRA_1843.
DR   KEGG; mra:MRA_1843; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_2_2_11; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000001988; 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..941
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045591"
FT   MOD_RES         692
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   941 AA;  99511 MW;  BFFDE54EDA56B914 CRC64;
     MSDHSTFADR HIGLDSQAVA TMLAVIGVDS LDDLAVKAVP AGILDTLTDT GAAPGLDSLP
     PAASEAEALA ELRALADANT VAVSMIGQGY YDTHTPPVLL RNIIENPAWY TAYTPYQPEI
     SQGRLEALLN FQTLVTDLTG LEIANASMLD EGTAAAEAMT LMHRAARGPV KRVVVDADVF
     TQTAAVLATR AKPLGIEIVT ADLRAGLPDG EFFGVIAQLP GASGRITDWS ALVQQAHDRG
     ALVAVGADLL ALTLIAPPGE IGADVAFGTT QRFGVPMGFG GPHAGYLAVH AKHARQLPGR
     LVGVSVDSDG TPAYRLALQT REQHIRRDKA TSNICTAQVL LAVLAAMYAS YHGAGGLTAI
     ARRVHAHAEA IAGALGDALV HDKYFDTVLA RVPGRADEVL ARAKANGINL WRVDADHVSV
     ACDEATTDTH VAVVLDAFGV AAAAPAHTDI ATRTSEFLTH PAFTQYRTET SMMRYLRALA
     DKDIALDRSM IPLGSCTMKL NAAAEMESIT WPEFGRQHPF APASDTAGLR QLVADLQSWL
     VLITGYDAVS LQPNAGSQGE YAGLLAIHEY HASRGEPHRD ICLIPSSAHG TNAASAALAG
     MRVVVVDCHD NGDVDLDDLR AKVGEHAERL SALMITYPST HGVYEHDIAE ICAAVHDAGG
     QVYVDGANLN ALVGLARPGK FGGDVSHLNL HKTFCIPHGG GGPGVGPVAV RAHLAPFLPG
     HPFAPELPKG YPVSSAPYGS ASILPITWAY IRMMGAEGLR AASLTAITSA NYIARRLDEY
     YPVLYTGENG MVAHECILDL RGITKLTGIT VDDVAKRLAD YGFHAPTMSF PVAGTLMVEP
     TESESLAEVD AFCEAMIGIR AEIDKVGAGE WPVDDNPLRG APHTAQCLLA SDWDHPYTRE
     QAAYPLGTAF RPKVWPAVRR IDGAYGDRNL VCSCPPVEAF A