ID   GCSP_PHOPR              Reviewed;         959 AA.
AC   Q6LHN5;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 104.
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=PBPRB1324;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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; CR378679; CAG23195.1; -; Genomic_DNA.
DR   RefSeq; WP_011221376.1; NC_006371.1.
DR   AlphaFoldDB; Q6LHN5; -.
DR   SMR; Q6LHN5; -.
DR   STRING; 298386.PBPRB1324; -.
DR   KEGG; ppr:PBPRB1324; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   Proteomes; UP000000593; Chromosome 2.
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:SF13; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 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..959
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227112"
FT   MOD_RES         707
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   959 AA;  104908 MW;  3155DFA0FF368910 CRC64;
     MTDMTLLNAL SDDQDFAGRH NGPNAAQQNI MLKAISAESV EQLIAQTVPA DIRLPEPMKL
     DPAQSEADML TSLKAIASKN IINRSYIGQG YYNNLTPNVV LRNVLENPGW YTAYTPYQPE
     ISQGRLESLL NYQQMIMDLT SMELANASLL DEATAAAEAM TLCLRAGKSK SKAFFVSNDL
     HPQTVDVVRT RAEYIGIEII TGSVEELDNH DVFGALVQYP GTTGSITDLT DIIEKAHAKK
     TLVAVASDLL ALTLLKAPGE MGADVVIGSA QRFGVPMGFG GPHAGFMATK DKHKRTMPGR
     VIGVSKDARG NQSLRMAMQT REQHIRREKA TSNICTAQAL LANMAAFYAL YHGPEGLRKI
     GRRVHHLTAI LAAGLRNSGI ELASDTFFDT ITLNTGKKTD DFYKKALAAG INLRKFDVQL
     GISLDETTKV SDVEELLAIF TGNKLKASMF TADIAADEFA AIPESCRRTS KYLTHPVFNE
     HHSETQMMRY MKKLENKDYS LTHGMIPLGS CTMKLNAAAE MIPITWPEFG SLHPFAPADQ
     TKGYQELASK LSEMLCSVTG YDAFSLQPNS GAQGEYAGLI AIQRYHQHNG DSHRNVCLIP
     SSAHGTNPAS AAMVSMKVVV VGCDEKGNVD VEDLKVKIEK HRDNLSCIMI TYPSTHGVYE
     EAVREVCDLV HDAGGQVYLD GANMNAQVGL TNPGFIGSDV SHLNLHKTFC IPHGGGGPGM
     GPIGVKSHLA PFLPGHVQST SDEGQQYAVS AAELGSASIL PISYAYIAMM GEEGLTEATK
     LAILNANYVM ERLRPHYPVL YRGTEGRIAH ECIIDIRPLK EASGISEEDV AKRLMDYGFH
     APTMSFPVAG TLMIEPTESE DLAELDRFCD AMIAIRQEIA RVQEGEWPID DNPLVHAPHT
     QADLMETEWN RAYSREIACF PTDHTRASKY WPTVNRVDNV FGDRNLICSC PSIDSYIED
//