ID   GCSP_PROMM              Reviewed;         962 AA.
AC   Q7V411;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=PMT_2169;
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
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; BX548175; CAE22343.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7V411; -.
DR   SMR; Q7V411; -.
DR   STRING; 74547.PMT_2169; -.
DR   EnsemblBacteria; CAE22343; CAE22343; PMT_2169.
DR   KEGG; pmt:PMT_2169; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_3; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000001423; 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; Reference proteome.
FT   CHAIN           1..962
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166924"
FT   MOD_RES         701
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   962 AA;  103971 MW;  1D11C9D97625A1AB CRC64;
     MRHIGPSLED QQQMLLELGH RDLQSFVAAV VPPDILETTA PSSSLPEGCG EVQAMEELRL
     IAAANRVRRS LIGLGYYGTA TPALIQRQVL ENPAWYTAYT PYQAEISQGR LEALFNFQTL
     ISELTGLPIA NASLLDEGTA AAEAMSLSFA ICKRPAAHRF LVDAEVLPQT LAVLRTRAEP
     LGIDLEVAEP MTFQFDAEVF GVLLQLPGRS GRLWDPTTSI QAAHEVGALA TVAIDPLAQV
     LLAPVAEFGA DIAVGSVQRF GVPMGFGGPH AAFFATLEIF KRQVPGRLVG QSVDAEGQPA
     LRLALQTREQ HIRRDKATSN ICTAQVLLAV MASFYAVHHG PDGLAAIARR VLRLRAQLER
     GLHQLGYPVQ SIARFDTIEV ICREAPAVHQ AAALAGFNLR VLPLGVAPEA AHGFGISFDE
     LSTDQELKSI LQILAEAAGQ PVPVLEDPGN PHLEELVGLP LRQRPWLQQQ VFHRYRSETE
     LLRYLQRLVG RDLSLVHGMI PLGSCTMKLN AAAELIPISW REFAALHPFA PQDQCQGYQR
     LVQDLEHWFA DITGFAGVSL QPNAGSQGEL AGLLVIRAWH HSRGEQQRDV CLIPTSAHGT
     NPATCVMAGL RVVPVACDAD GNVDLNDLAS KAEAHAPQLA ALMVTYPSTH GVFEPQIREI
     CELVHGHGGQ VYLDGANLNA QIGFCRPGTY GADVCHINLH KTFCIPHGGG GPGVGPIAVS
     AHLMPFLPGH PLAACGGEQG IGAISAAPWG SAGILPISWM YLRMMGAEGL RQASAVALLS
     ANYLAHRLHP HYPVLFRGQA GLVAHECILD LRPLKRSAGL EVDDIAKRLM DYGFHAPTVS
     WPVAGTVMVE PTESESLEEL NRFCDAMIAI REETAAIESG QIDPQNNPLR RAPHTLAAVT
     AEVWDRPYSR AEAAFPLAEQ RQSKFWPAVS RIDNAYGDRN LLCSCPSVEE LADNAVLKPP
     LV