ID   GCSP_GRAFK              Reviewed;         949 AA.
AC   A0M5D4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   25-MAY-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=GFO_2875;
OS   Gramella forsetii (strain KT0803).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Gramella.
OX   NCBI_TaxID=411154;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT0803;
RX   PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA   Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA   Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA   Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA   Gloeckner F.O.;
RT   "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT   reveals adaptations to degradation of polymeric organic matter.";
RL   Environ. Microbiol. 8:2201-2213(2006).
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; CU207366; CAL67829.1; -; Genomic_DNA.
DR   RefSeq; WP_011710730.1; NC_008571.1.
DR   AlphaFoldDB; A0M5D4; -.
DR   SMR; A0M5D4; -.
DR   STRING; 411154.GFO_2875; -.
DR   EnsemblBacteria; CAL67829; CAL67829; GFO_2875.
DR   KEGG; gfo:GFO_2875; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_10; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000000755; 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.
FT   CHAIN           1..949
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045584"
FT   MOD_RES         700
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   949 AA;  104980 MW;  4C244DFB5570E1DB CRC64;
     MRTDSFALRH IGPKAENLQE MLDTIGVESI EQLIYETIPD DIRLDQPLNL PKAMSENQYA
     EHIKKLSEKN RVFKTYIGLG YHQAILPAVI QRNILENPGW YTAYTPYQAE IAQGRLEALL
     NFQTMVSDLT GMEIANASLL DESTAAAEAM ALLHAVRDRK QKKDDVNKFF VSQQTLPQTI
     SLMETRANFL GIDMVVGDHE EFDFSEEYFG ALVQYPGKFG QIFDYANFVE NCKNANIKTA
     FAADILSLVK LQAPGELGVD VVVGTTQRFG IPLGYGGPHA AYFATKEEYK RNLPGRIIGL
     TKDLDGNNAL RMALQTREQH IKRDKATSNI CTAQVLLAVM AGMYAVYHGP KGLEYIANIV
     HASAVSLEDS LKELGFEQLN SAYFDTIHVK ANASKLKAIA EKHEINFFYP DAESACISIN
     ETTTTDDLNA VIAVFAELSE KKHAEIEELS ERTAIPKNLE RKTEFLTHEV FNLYHSETEL
     MRYIKKLERK DLSLNHSMIS LGSCTMKLNA ASEMLPLSNP QWGNMHPFAP VNQAEGYQTV
     LKELEHQLTE ITGFSATSLQ PNSGAQGEYA GLMVIRAYHE ANGEGHRNVC LIPSSAHGTN
     PASAVMAGMK VVVTKASENG NIDVDDLREK AIKHKDNLAA LMVTYPSTHG VFESAIREIT
     NIIHENGGQV YMDGANMNAQ VGLTNPGRIG ADVCHLNLHK TFAIPHGGGG PGVGPICVAE
     QLKPFLPGNP VIKTGGEKAI GAISSAPWGS SLVCLISYGY IKMLGTGGLQ QATEYAILNA
     NYIKARLNDH YKTLYSGERG RAAHEMIIDC RPFKEQGIEV TDIAKRLIDY GFHSPTVSFP
     VAGTMMIEPT ESESKPELDR FCDALISIRK EIDEVSVDDS NNVLKNAPHT IHMLTSDEWK
     LPYSREKAAY PLDHLHDNKF WPSVRRVDEA FGDRNLMCTC PPTEEYAEA