ID   GCSP_NOCFA              Reviewed;         934 AA.
AC   Q5YWV4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 113.
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=NFA_24900;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
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; AP006618; BAD57337.1; -; Genomic_DNA.
DR   RefSeq; WP_011209022.1; NC_006361.1.
DR   AlphaFoldDB; Q5YWV4; -.
DR   SMR; Q5YWV4; -.
DR   STRING; 247156.NFA_24900; -.
DR   GeneID; 61133238; -.
DR   KEGG; nfa:NFA_24900; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_2_1_11; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000006820; 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; 3.90.1150.10; 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; Reference proteome.
FT   CHAIN           1..934
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227110"
FT   MOD_RES         687
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   934 AA;  99249 MW;  3D1FE2DBA0B7A6F8 CRC64;
     MTRSFADRHI GPDAAELSRI LEVVGVDSLD ALAAAALPAS ILDDAGAGPL AALPPAVSEH
     EALAELAALA QSNTVTTSMI GLGYYDTLTP PVLVRNLLEN PAWYTAYTPY QPEISQGRLE
     ALLNFQTMVS DLTGMEVANA SMLDEATAAA EAMTLLRRAG RSRSNRLLID ADLFPQTRTV
     LHTRAEPLGI EIVEADLAAA GLPEGGFFGV IVQVPGASGR VVDWTALIAA AHERGALVAA
     GADLLAMTLI VPPGEQGADV CFGTTQRFGV PMGFGGPHAG YLAVRSAHAR QLPGRLVGVS
     KDADGNPAYR LALQTREQHI RREKATSNIC TAQVLLAIVA AMYACYHGAD GLRAIARRVH
     GHAARIAGAL GEALVHDTYF DTVLARVPGH AEAVVAKAAA CGITLRLVDP DHVAVACDEA
     TTDAHVEAVL DAFGVAPAEP VDAGIATRTS EFLTHPAFTR YRTETAMLRY LRSLSDKDIA
     LDRSMIPLGS CTMKLNATAE MEPITWPGFA KLHPYAPVEH APGLLKLIGD LESWLAEITG
     YDAVSLQPNA GSQGEYAGLL AIRRYHLDRG DTHRDTCLIP SSAHGTNAAS AAMAGLRVEV
     VKCRENGDVD LDDLRAKITD HAERLACIMI TYPSTHGVYE HEIAELCALV HDAGGQVYVD
     GANLNALVGL ARPGRFGGDV SHLNLHKTFC IPHGGGGPGV GPVAVRAHLA QYLPGDPLES
     GSHAVSAARY GSASILPITW AYIRMMGAEG LRKATLTAIA SANYLARRLD EYFPVLYTGE
     NGMVAHECIL DLRELTKRTG VTVDDVAKRL ADYGFHAPTM SFPVAGTLMV EPTESENLAE
     LDEFVAAMIA IRAEIDQVGA GVWPAEDNPL RGAPHTAECL VGEWTHPYSR EIAVYPRGLG
     HARAKVWPAV RRIDGAYGDR NLVCSCPPLE AYAE
//