ID   GCSP_PELUB              Reviewed;         952 AA.
AC   Q4FMV1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=SAR11_0668;
OS   Pelagibacter ubique (strain HTCC1062).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Pelagibacterales;
OC   Pelagibacteraceae; Candidatus Pelagibacter.
OX   NCBI_TaxID=335992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC1062;
RX   PubMed=16109880; DOI=10.1126/science.1114057;
RA   Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA   Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA   Carrington J.C., Mathur E.J.;
RT   "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL   Science 309:1242-1245(2005).
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; CP000084; AAZ21488.1; -; Genomic_DNA.
DR   RefSeq; WP_011281853.1; NC_007205.1.
DR   AlphaFoldDB; Q4FMV1; -.
DR   SMR; Q4FMV1; -.
DR   STRING; 335992.SAR11_0668; -.
DR   EnsemblBacteria; AAZ21488; AAZ21488; SAR11_0668.
DR   GeneID; 66295172; -.
DR   KEGG; pub:SAR11_0668; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_5; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000002528; 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..952
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227111"
FT   MOD_RES         696
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   952 AA;  106007 MW;  106AE6F72ABC7B87 CRC64;
     MLKNAQKDFI QRHIGPSVDE QNVMLKELGY QNLDDLIKDT VPEKILLKDD LDIGDPNSEY
     KALRKLKDIS KKNKIYSSFI GMGYYGTYTP YVILRNILEN PGWYTSYTPY QPEVAQGRLE
     MLLNFQQMII DFTGMDIANA SLLDEGTAAA EAMGLSYRIS KSESKKVFVS KNCHPQTIDV
     IKTRAEPLGL EIIVGDEDKD IKEDIICGII QYPGTLGDIK DPSEAISKIH KFNGKAVLAC
     DLLALAKLKT PAELGADIAV GSSQRFGIPM GYGGPHAAFF ATKDEYKRSM PGRIVGVSVD
     RHGKKAYRLA LQTREQHIRR DKATSNICTA QALLAIVSAA YAVYHGPQGI KKIAESVSQL
     TKNFADKLKQ SGYELYSNEF FDTVTIKTLD KTEKIYKNAL DQGVNIRKVN SEMLAVSFDE
     RKNLYRANQL LKIFNCSETI KETMNESLSN IPKNLLRTST YLDHPVFNSY HSETEMLRYL
     KKLEDSDIAL NKSMIALGSC TMKLNAVAEM IPVTWKEFSQ PHPFSPVEQM DGYRELFTDL
     KNWLRSITGF SGVSLQPNAG AQGEFAGLMV IRKFHEKNGE TNRNVCLIPS SAHGTNPASA
     QMVGMKVVVV KCDQYGNVDY EDLKNKAEEH SENLAALMVT YPSTHGVFEE KITDICELIH
     NHGGQVYMDG ANLNALVGIA KPGNFGPDVC HINLHKTFCI PHGGGGPGMG PIACKKHLEI
     FLPKHSVIKD CGPVTGMGAV SAAPWGSSSI LSISWMYIKM MGSEGLRKAS QVAILNANYI
     AHKLKDSFPI LYKGKSGNVA HECIIDIRTI KSETGITEED IAKRLIDFGY HAPTMSWPVA
     GTMMIEPTES ESLSEIDKFC STLIKIKQEI DKIQSGEYDK TDNPLKNAPH THVELTSNKW
     DHKYEREEAA YPSEFLRTNK YWPPVGRVDN VYGDKNLFCT CPSMEEYEDT AA