ID   GCSP_IDILO              Reviewed;         962 AA.
AC   Q5R192;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, 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}; OrderedLocusNames=IL2092;
OS   Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Idiomarina.
OX   NCBI_TaxID=283942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX   PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA   Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA   Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA   Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA   Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT   "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT   loihiensis reveals amino acid fermentation as a source of carbon and
RT   energy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(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; AE017340; AAV82924.1; -; Genomic_DNA.
DR   RefSeq; WP_011235320.1; NC_006512.1.
DR   AlphaFoldDB; Q5R192; -.
DR   SMR; Q5R192; -.
DR   STRING; 283942.IL2092; -.
DR   KEGG; ilo:IL2092; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000001171; 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: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..962
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227106"
FT   MOD_RES         710
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   962 AA;  105779 MW;  197029FEC1EB7982 CRC64;
     MSSTTLTQLE HHDEFISRHI GPSADEQKAM LAELGVDSLE ALTKDTVPGA ILREPFLQTG
     EPQTEREALA RLKNIAKKNQ ICTSYIGMGY YDTVVPNVIL RNVLENPGWY TAYTPYQPEI
     AQGRLEALLN FQQMTMDLTG LDLASASLLD EATAAAEAMA MAKRVSKNKK SNAFFIADNV
     YTQTIDVVKT RAEYFGFDII VGPAREASDH DVFGALLQYP DKQGQLHNIE QLIGELQEKK
     AIVAVASDLM SLLMVKSPGE MGADMVFGNA QRFGVPMGYG GPHAAFFATR DKFKRSLPGR
     IIGVSKDSRG RPALRMAMQT REQHIRREKA NSNICTAQVL LANMASFYAV YHGPDGLRRI
     ANRIHRLTDI VALGMQDKGV KLVNSHWFDT LTFEMKENAA DVLARSKALG LNLRVDGEGM
     FGISLDEAKT RDDVESLFAA LFGDNHGLDI DVLDSRVAGG DVESIPADLV RQSQYLQHPV
     FNEYHSETEM LRYIKKLENK DLALNHSMIS LGSCTMKLNA TAEMIPVTWP EFGQLHPFCP
     AEQAQGYYEL VSTLSEWLID VTGYDAMSMQ PNSGAQGEYA GLLAIQKYHE SRGDGHRNIC
     LIPSSAHGTN PASAQMMNMK VVVVDCDKHG NVDMDDLKAK AEEAGENLSC IMVTYPSTHG
     VYEEGIKDIC DLVHNYGGQV YMDGANMNAQ VGVTSPGYIG SDVSHLNLHK TFCIPHGGGG
     PGMGPIGVKQ HLAEFLPNHS IVNIDGPKAG NGAVSAAQFG SASILTISWM YIAMMGGRGL
     REASETAILN ANYLAEKLSK HFKILYRGRN NRVAHECIID LRPMKDAAGI AEIDVAKRLQ
     DYGFHSPTMS FPVAGTIMVE PTESESKAEL DRFIEALVSI KAEAEKVAAG EWPKDNNPLV
     NAPHTLADIT DAEWDRPYDR KTATYPVEAV GYDKFWPTVN RIDDVFGDRN LMCSCPSIEE
     YR
//