ID   GCSP_PROM3              Reviewed;         982 AA.
AC   A2CDR0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=P9303_28901;
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000554; ABM79620.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2CDR0; -.
DR   SMR; A2CDR0; -.
DR   STRING; 59922.P9303_28901; -.
DR   EnsemblBacteria; ABM79620; ABM79620; P9303_28901.
DR   KEGG; pmf:P9303_28901; -.
DR   HOGENOM; CLU_004620_3_2_3; -.
DR   OMA; CVPMSEY; -.
DR   BioCyc; PMAR59922:G1G80-2533-MON; -.
DR   Proteomes; UP000002274; 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; 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..982
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000147968"
FT   MOD_RES         721
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   982 AA;  106280 MW;  FD1E911438C2C33F CRC64;
     MTLLEQRAVE ASSIQSSPFL VRHIGPSFED QQQMLLELGH RDLQSFVAAV VPPDILETTA
     PTSSLPEGCG EVQAMEELRL IAAANRVRRS LIGLGYYGTA TPALIQRQVL ENPAWYTAYT
     PYQAEISQGR LEALFNFQTL ISELTGLPIA NASLLDEGTA AAEAMSLSFA ICKRPQAHRF
     LVDAEVLPQT LAVLRTRAEP LGIHLEVAEP MTFQFDAEVF GVLLQLPGRS GRLWDPTTSI
     QAAHEVGALA TVAIDPLAQV LIAPVAEFGA DIAVGSVQRF GVPMAFGGPH AAFFATLEIF
     KRQVPGRLVG QSVDAEGQPA LRLALQTREQ HIRRDKATSN ICTAQVLLAV MASFYAVHHG
     PDGLAAIARR VLLLRAQLER GLHQLGYPVQ SIARFDTIEV ICREAPAVHQ AAALAGFNLR
     VLPLGVAPEA AHGFGISFDE LSTDQELKSI LQILAEAAGQ PVPVLEDLGN PHLEELVGLP
     LRQRPWLQQQ VFHRYRSETE LLRYLQRLVG RDLSLVHGMI PLGSCTMKLN AAAELIPISW
     REFAALHPFA PQDQCHGYQR LVQDLEHWFA EITGFAGVSL QPNAGSQGEL AGLLVIRAWH
     HSRGEQQRDV CLIPTSAHGT NPATCVMAGL RVVPVACDAE GNVDLNDLAS KAEAHAPQLA
     ALMVTYPSTH GVFEPQIREI CELVHGHGGQ VYLDGANLNA QIGFCRPGTY GADVCHINLH
     KTFCIPHGGG GPGVGPIAVA AHLMPFLPGH PLAACGGEQG IGAISAAPWG SAGILPISWM
     YLRMMGAEGL RQASAVALLS ANYLAHRLHP HYPVLFRGQA GLVAHECILD LRPLKRSAGL
     EVDDIAKRLM DYGFHAPTVS WPVAGTVMVE PTESESLEEL NRFCDAMIAI REETAAIESG
     QIDPQNNPLR RAPHTLAAVT AEVWDRPYSR AEAAFPLAEQ RQSKFWPAVS RIDNAYGDRN
     LLCSCPSVEE LADNSVLKPP LV