ID   GCSP_RHOPA              Reviewed;         990 AA.
AC   Q6N344;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=RPA3850;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
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; BX572605; CAE29291.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6N344; -.
DR   SMR; Q6N344; -.
DR   STRING; 258594.RPA3850; -.
DR   PRIDE; Q6N344; -.
DR   EnsemblBacteria; CAE29291; CAE29291; RPA3850.
DR   KEGG; rpa:RPA3850; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_2_1_5; -.
DR   OMA; CVPMSEY; -.
DR   PhylomeDB; Q6N344; -.
DR   Proteomes; UP000001426; 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..990
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227125"
FT   MOD_RES         726
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   990 AA;  106401 MW;  BB35BA120F969DFF CRC64;
     MTPLRFPSNL PLRAVAFDED QSMPHRRPID AANDFVRRHI GPSPQDIAAM LATAGAGSLE
     QLVAETLPYA IRHREPLKLG APLTESEALA HMSELGAQNQ VFTSLIGQGY YGTILPTVIQ
     RNILENPAWY TAYTPYQPEI SQGRLEALFN FQTMICDLTG LDVANASLLD EGTAAAEAMA
     LAERAAAKNA KAFFVDADTH PQTIAVLRTR AEPLGWRIIV GNPETGLEGA DVFGALLQYP
     GSSGRLSDPR AVIAALRKKG ALAVVAADLL ALTLITPPGE LGADIAIGSA QRFGVPMGYG
     GPHAAYMAVR DSLKRSLPGR IVGLSIDSHG QPAYRLALQT REQHIRREKA TSNICTAQVL
     LAVINAMYAV YHGPDGLAAI ARRVHRRTAV LAAGLQQLGF APTHGNYFDT LTIEVGDRRD
     AIVARAEAEN INLRINASSL GISLDETTTP ATVEALWRAF GGSLDYAAVE RDAGDALGTA
     LPAALKRTSD YLTQPAFQDY RSETELLRYM RKLSDRDLAL DRAMIPLGSC TMKLNATTEM
     MPLTWPEFGS LHPFVPKAQA AGYHALFERL ETWLAEITGY DAVSLQPNSG AQGEYAGLLT
     IRGYHLSRGE PHRKVCLIPS SAHGTNPASA AMAGMDVVVV ACDAHGDVDV DDLRAKAEAH
     SADLAAVMIT YPSTHGVFEE HIREICDIVH AHGGQVYLDG ANLNAQVGLA RPGSYGADVS
     HLNLHKTFCI PHGGGGPGMG PIGVKAHLAP FLPGHPAEGE PLNGGLHGGG TVSAAPWGSA
     SILTISYIYI LMMGAAGLKR ATEIAILNAN YIAAKLHPHF PVLYRNPRGR VAHECIIDPR
     ALKTSTGVTV DDIAKRLIDY GFHAPTMSFP VPGTLMIEPT ESESKAEIDR FCDAMIAIRR
     EIAQVEAGRY PIEQSPLRHA PHTAHDVTSA EWTRPYPRTE GCFPAPNSRT DKYWSPVGRV
     DNVYGDRNLI CSCPPVEDYA LAADYARAAE