ID   GCSP_PROMT              Reviewed;         968 AA.
AC   Q46IC1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=PMN2A_1267;
OS   Prochlorococcus marinus (strain NATL2A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL2A;
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; CP000095; AAZ58757.1; -; Genomic_DNA.
DR   RefSeq; WP_011295611.1; NC_007335.2.
DR   AlphaFoldDB; Q46IC1; -.
DR   SMR; Q46IC1; -.
DR   STRING; 59920.PMN2A_1267; -.
DR   EnsemblBacteria; AAZ58757; AAZ58757; PMN2A_1267.
DR   KEGG; pmn:PMN2A_1267; -.
DR   HOGENOM; CLU_004620_2_1_3; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   PhylomeDB; Q46IC1; -.
DR   Proteomes; UP000002535; 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..968
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227113"
FT   MOD_RES         712
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   968 AA;  107029 MW;  79DDE59B3D0F6780 CRC64;
     MSKAELKDFT FKSRHIGPTN EDEALMLQHL GYENAEEFIS SVIPNEIFDS ENNGVSIPDG
     CDQNKALTEI NIISKKNVEH RSLIGLGYHS TVIPPVIQRN VLENPNWYTA YTPYQAEISQ
     GRLEALFNFQ TLISELTGLP ISNASLLDEA TAAAEAISLS LTVRKNKNAN KFLVDQEILP
     QTLDVLKTRC EPLGISLEMF DNNNFEIDKN VFGILIQLPG KNGRIWDPTK IINDAHKCNA
     IVTIAIDPLA QVLIKPMGEF GADIVVGSAQ RFGVPIAFGG PHAAFFATKE IYKRQIPGRI
     VGQSVDVEGN QALRLALQTR EQHIRRDKAT SNICTAQVLL AVLSSFYAVH HGPKGLKQIA
     ENVVKYRSNF ESILMNLEYP IEKYSAFDSV DVYCSEASEV IQLASEEGYN LRVLPIGSDF
     ENAKGFGVTF DELTCDEEIY KLHQILAQVK GKKTHDLSNF IFENASLIDI PLREKSWLEQ
     SVFNQYQSET DLMRYIHCLV SKDFSLVQGM IPLGSCTMKL NAAAELLPIE WREFSSIHPF
     APHTQLTGFH EIINDLENWL SALTGFQGVS LQPNAGSQGE FAGLLVIRSW HQSLGEGHRN
     ICLIPTSAHG TNPASAVMSG FKVVSVKCDE YGNVDLEDLK NKSKIHSKNL AALMVTYPST
     HGVFEPNIRE MCQVIHQEGG QVYLDGANLN AQVGICRPGS YGIDVCHLNL HKTFSIPHGG
     GGPGVGPIAV ADHLVPYLPG HSIIKCGGQK AISAVSAAPF GSAGILPISW MYIRMMGSDG
     LRKASSIAIL SANYLAKRLD PYYPVLFKDP NGLVAHECIL DLRPLKSQLG IEVEDVAKRL
     MDYGFHAPTI SWPVAGTLMV EPTESESLPE LDRFCDAMIG IREEIEQIKL GKIDPINNPL
     KQSPHTLKTV TSDDWDRPYS RKEAAYPLPD QEKYKFWPSV SRINNAYGDR NLICSCPSVQ
     DLEDINSV