ID   GCSP_RHOFA              Reviewed;         949 AA.
AC   Q8G9M2;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 66.
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};
DE   Flags: Fragment;
GN   Name=gcvP {ECO:0000255|HAMAP-Rule:MF_00711}; Synonyms=gcvB;
OS   Rhodococcus fascians.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1828;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D188;
RX   PubMed=11807072; DOI=10.1128/jb.184.4.1112-1120.2002;
RA   Vereecke D.M., Cornelis K., Temmerman W., Jaziri M., Van Montagu M.,
RA   Holsters M., Goethals K.;
RT   "Chromosomal locus that affects pathogenicity of Rhodococcus fascians.";
RL   J. Bacteriol. 184:1112-1120(2002).
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; AJ301559; CAD52982.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8G9M2; -.
DR   SMR; Q8G9M2; -.
DR   STRING; 1443905.GCA_000761075_02925; -.
DR   PRIDE; Q8G9M2; -.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR   CDD; cd00613; GDC-P; 1.
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..949
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166933"
FT   MOD_RES         702
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
FT   NON_TER         1
SQ   SEQUENCE   949 AA;  100704 MW;  870E324050C6380A CRC64;
     TDRMTSTASA FVDRHVGPDT TELARILDAI GVDSLDELAR KAVPESILDT VVDGVPDGLA
     TLPPALSEHD ALAALADLAG CNTVATSMIG LGYYDTLTPP VLTRGILENP AWYTAYTPYQ
     PEISQGRLEA LLNFQTMVSD LTGMDVANAS MLDESTAAAE SMTLMRRANR GSKSPRLVVD
     SDIFPQTKAV LATRAEPLGI ELVYADLADG LPEGDFFGVL AQLPGASGRL VDHTATIEAA
     HERGALVAVG VDLLAATLVT APGEIGADVC FGTTQRFGVP MGYGGPHAGY LAVRSGHSRQ
     LPGRLVGVSV DADGHRAYRL ALQTREQHIR REKATSNICT AQVLLAIVAA MYASYHGADG
     LRAIARRVNT RARTVAAGLQ AAGIDVVHAE FFDTVLAAVP GAAHTVVDAA KQRGINLRPV
     DDDHVAIACD EATTEAHIVD VLAAFGAEPA GPGAESVPAD CARTSEYLTH PAFTRYRTET
     AMLRYLRALS DKDIALDRSM IPLGSCTMKL NATAEMESIT WPQFARQHPF APSTDVPGLL
     RVIADLEQWL VDITGYDAVS LQPNAGSQGE YAGLLAIRRY HQANGDTGRT VCLIPSSAHG
     TNAASAVMVG MRVVVVACRP NGDVDVDDLR AKIAEHADTL AAIMITYPST HGVYEHEISD
     ICAAVHDAGG QVYVDGANLN ALVGLARPGR FGGDVSHLNL HKTFCIPHGG GGPGVGPIGV
     RSHLQPYLPG HPLAPQLGDG PTVAGAPYGS ASILTITWAY IAMMGAQGLR RATLTAIASA
     NYIARRLDEY FPVLYTGDNG MVAHECILDL RGLTKDTGVT VDDVAKRLAD YGFHAPTMSF
     PVPGTLMVEP TESENLEEID AFCDAMISIR REIDRVGSGE WTVEDNPLRG APHTAQCLVA
     DWNHPYSREL AAYPAGYDRP KVWPAVRRID GAHGDRNLVC SCPPIEAFA