ID   GCSP_PROM1              Reviewed;         968 AA.
AC   A2C5D4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=NATL1_21381;
OS   Prochlorococcus marinus (strain NATL1A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL1A;
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; CP000553; ABM76694.1; -; Genomic_DNA.
DR   RefSeq; WP_011824632.1; NC_008819.1.
DR   AlphaFoldDB; A2C5D4; -.
DR   SMR; A2C5D4; -.
DR   STRING; 167555.NATL1_21381; -.
DR   EnsemblBacteria; ABM76694; ABM76694; NATL1_21381.
DR   KEGG; pme:NATL1_21381; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_2_1_3; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000002592; 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..968
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045594"
FT   MOD_RES         712
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   968 AA;  107028 MW;  84FEBA73081CEF65 CRC64;
     MSKAELKDFT FKSRHIGPTN EDEALMLQHL GYENSEEFIS SVIPNEIFDS ENNVVSIPDG
     CDQNKALKEI NIISKKNVEH RSLIGLGYHS TVIPPVIQRN VLENPNWYTA YTPYQAEISQ
     GRLEALFNFQ TLISELTGLP ISNASLLDEA TAAAEAISLS LAVRKNKNAN KFLVDQEILP
     QTFDVLKTRC EPLGISLEMF ENNNFEIDKN IFGILIQLPG KNGRIWDPTK IINDAHKCNA
     IVTIAIDPLA QVLIKPMGEF GADIVVGSAQ RFGVPIACGG PHAAFFATKE IYKRQIPGRI
     VGQSVDVEGN QALRLALQTR EQHIRRDKAT SNICTAQVLL AVLSSFYAVH HGPKGLKQIA
     ENVVKYRSNF ESILMNLEYP IEKYSAFDSV DVYCSEASEV IQLASEEGYN FRVLPIGSDF
     ENAKGFGVTF DELTCDEEIY TLHQILAQVK GKKAHDLSNF LNENASLVDI PLREKSWLEQ
     SVFNQYQSET DLMRYIHSLV SKDFSLVQGM IPLGSCTMKL NSAAELLPIE WREFSSIHPF
     APHAQLAGFH EIINDLENWL SALTGFQGVS LQPNAGSQGE FAGLLVIRSW HQSLGEGHRN
     ICLIPTSAHG TNPASAVMSG FKVVSVKCDE YGNVDLEDLK NKSKIHSKNL AALMVTYPST
     HGVFEPNIRE MCQVIHQEGG QVYLDGANLN AQVGICRPGS YGIDVCHLNL HKTFSIPHGG
     GGPGVGPIAV ADHLVPYLPG HSIIKCGGEK AISAVSAAPF GSAGILPISW MYIRMMGSDG
     LRKASSIAIL SANYLAKRLD PYYPVLFKDP NGLVAHECIL DLRPLKSQLG IEVEDVAKRL
     MDYGFHAPTI SWPVAGTLMV EPTESESLPE LDRFCDAMIG IREEIEQIKL GKIDPINNPL
     KQSPHTLKRV TSDDWDRPYS RKEAAYPLPD QEKYKFWPSV SRINNAYGDR NLICSCPSVQ
     DLEDINSV