ID   GCSP_MYCGI              Reviewed;         952 AA.
AC   A4TA90;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 107.
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};
GN   OrderedLocusNames=Mflv_3398;
OS   Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS   PYR-GCK)).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYR-GCK;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium gilvum PYR-GCK.";
RL   Submitted (APR-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=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; 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; CP000656; ABP45874.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4TA90; -.
DR   SMR; A4TA90; -.
DR   STRING; 350054.Mflv_3398; -.
DR   KEGG; mgi:Mflv_3398; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_2_1_11; -.
DR   OrthoDB; 9801272at2; -.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR003437; GcvP.
DR   InterPro; IPR049316; GDC-P_C.
DR   InterPro; IPR049315; GDC-P_N.
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   NCBIfam; TIGR00461; gcvP; 1.
DR   PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate.
FT   CHAIN           1..952
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000083209"
FT   MOD_RES         703
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   952 AA;  100876 MW;  CBB4069F4EFB2A68 CRC64;
     MPDQTPAPSV LRFVDRHIGP DDQAVETLLN TIGVPSLDEL AAKALPDVIL DRLSTDGVAP
     GLEHLPAAAT EHEALAELRA LAQSNTVAVS MIGQGYYDTL TPPVLRRNII ENPAWYTAYT
     PYQPEISQGR LEALLNFQTM VTDLTGLEVA NASMLDEGTA AAEAMTLMHR AVRGPATRLA
     VDADVYPQTA AILATRAEPL GIEIVTADLR QGLPDGDFFG VIVQLPGASG VVHDWSALVE
     QAHERGALVA VGADLLAATM ITPPGEIGAD VAFGTTQRFG VPMGFGGPHA GYLAVHSKHA
     RQLPGRLVGV SVDADGSRAY RLALQTREQH IRRDKATSNI CTAQVLLAVL AAMYASYHGP
     DGLRGIAQRV HGHARALAAG LADAGVEVVH DSFFDTVLAH VPGRADEVRA AAKERGINVW
     AVDADHVSVA CDEATTAEHV ADVLAAFGAA PSGADFAGPA VATRTSEFLT HPAFSDYRTE
     TSMMRYLRSL ADKDIALDRS MIPLGSCTMK LNAAAEMEAI TWAEFGRQHP FAPASDTPGL
     RRLIADLQSW LTGITGYDEI SLQPNAGSQG EYAGLLAIQA YHHARGDSGR TVCLIPSSAH
     GTNAASAAMV GMKVVVVACR ANGDVDLDDL RAKVTEHADR LSALMITYPS THGVYEHDIA
     DICAAVHDAG GQVYVDGANL NALVGLARPG RFGGDVSHLN LHKTFCIPHG GGGPGVGPVA
     VRAHLAPYLP GHPLAAELSD DHTVSAAPYG SASILPITWA YIRMMGAAGL RSATLVAIAS
     ANYIARRLDE YYPVLYTGEN GMVAHECILD LRGITKATGV TVDDVAKRLA DYGFHAPTMS
     FPVAGTLMVE PTESESLSEI DAFCDAMIAI RAEIDRVGSG EWPVDDNPLR GAPHTAESLL
     VEEWTHPYTR EQAAYPLGKG FRPKVWPPVR RIDGAYGDRN LVCSCPPVEA FA
//