ID   GCSP_PROMA              Reviewed;         964 AA.
AC   Q7V9K4;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=Pro_1829;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(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; AE017126; AAQ00873.1; -; Genomic_DNA.
DR   RefSeq; NP_876220.1; NC_005042.1.
DR   RefSeq; WP_011125978.1; NC_005042.1.
DR   AlphaFoldDB; Q7V9K4; -.
DR   SMR; Q7V9K4; -.
DR   STRING; 167539.Pro_1829; -.
DR   EnsemblBacteria; AAQ00873; AAQ00873; Pro_1829.
DR   GeneID; 54201159; -.
DR   KEGG; pma:Pro_1829; -.
DR   PATRIC; fig|167539.5.peg.1931; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_0_3; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000001420; 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; 3.40.640.10; -; 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..964
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166923"
FT   MOD_RES         711
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   964 AA;  106218 MW;  B2452DAF167A1695 CRC64;
     MRNTKASKFS DRHLGLIEEA QVEILNALGH ADINDFISSV VPEEILDAQP PDELLPKALN
     EIEALEELRS IAKKNQIKRS LIGLGYYGTY TPAVIQRHVF ENPAWYTSYT PYQAEIAQGR
     LEALFNFQTL ITELTGLPIA NASLLDEGTA AAEAMSLSFA VNKQTKARKF IVDDQVLPQT
     LAVLKTRAEP LELDIEVVNL TDLVINETVF GLLIQLPGKS GQLWDPSSLI AQAHEFNALV
     TVAIDPLAQV LIAPMGQLGV DIAIGSSQRF GVPIGFGGPH AAFFAIKEEY KRLVPGRLVG
     QSIDSKGHSA LRLALQTREQ HIRRDKATSN ICTAQALLAT IASFYAVYHG PHGLEEIAKN
     IIYLRSQLEL YLKEFGYTFA PDCRFDTLEI HCLEAPEIHR LSILSGFNLR ILPLGASIEK
     SKGFAVSFDE LSTTKELYKL CKIFADVKDK NFEPRENTNF NFKESLTSLP LRTTPWLKQQ
     VFNNYRTETE LMRYIQKLAS RDFSLVNGMI PLGSCTMKLN ATAELLPITW KEFSSIHPFV
     PSDQAKGYGY LSEQLEGWLC ALTGFDGVSL QPNAGSQGEF AGLLVIRAWH KAINQADRNI
     CLIPKSAHGT NPASAVMAGF KVVAVECDEY GNIDFEDLVL KVETYSSELG ALMITYPSTH
     GVFEPNIRQI CDQVHLHGGQ VYLDGANLNA QVGLCRPGAF GADVCHLNLH KTFCIPHGGG
     GPGIGPIAVA KHLVAFLPSK NFHASDNNAA IGAISASPLG SASILPISWM YIRMMGADGL
     RQASSLAILS ANYIANKLDP YFQVLFKAPN GKVAHECILD LRSIKRITGI EVDDVAKRLM
     DYGFHAPTIS WPVAGTLMIE PTESESFEEI NRFCEAMISI RSEIDAIESG ITDLSNNPLR
     LAPHTMETVT AEIWDRPYTR QQAAFPLKDQ FMNKFWPAVS RIDNAFGDRN LVCSCSTLEE
     LSET