ID   GCSP_DINSH              Reviewed;         954 AA.
AC   A8LIH2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Dshi_2680;
OS   Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Dinoroseobacter.
OX   NCBI_TaxID=398580;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16493 / NCIMB 14021 / DFL 12;
RX   PubMed=19741735; DOI=10.1038/ismej.2009.94;
RA   Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I.,
RA   Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., Han C.,
RA   Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., Liebl W.,
RA   Liesegang H., Meincke L., Pati A., Petersen J., Piekarski T.,
RA   Pommerenke C., Pradella S., Pukall R., Rabus R., Stackebrandt E., Thole S.,
RA   Thompson L., Tielen P., Tomasch J., von Jan M., Wanphrut N., Wichels A.,
RA   Zech H., Simon M.;
RT   "The complete genome sequence of the algal symbiont Dinoroseobacter shibae:
RT   a hitchhiker's guide to life in the sea.";
RL   ISME J. 4:61-77(2010).
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; CP000830; ABV94413.1; -; Genomic_DNA.
DR   RefSeq; WP_012179341.1; NC_009952.1.
DR   AlphaFoldDB; A8LIH2; -.
DR   SMR; A8LIH2; -.
DR   STRING; 398580.Dshi_2680; -.
DR   PRIDE; A8LIH2; -.
DR   EnsemblBacteria; ABV94413; ABV94413; Dshi_2680.
DR   KEGG; dsh:Dshi_2680; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_5; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000006833; 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..954
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000083205"
FT   MOD_RES         700
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   954 AA;  103117 MW;  1603D6202E390F42 CRC64;
     MGFSLTDYAP YDFANRRHIG PSPKEMGQML ATLGVPSLEA LINEALPEGI RRRDPLAFGP
     ALSERDTLHR MRELADKNTV LTSLIGQGYH GTHTPPVILR NILENPAWYT AYTPYQPEIS
     QGRLEALLNF QTMMADLTGL PIANASLLDE GTAAAEAMAM AQRASKSKAR GFFVAEDCHP
     QTIDVIRTRA EPLGIEVIVG AVDALDPEAV FAALFQYPGS YGHVRDYSDV IEALHGARAL
     AVVAADPLAL TLLKSPGEMG ADIAIGSTQR FGVPMGYGGP HAAYMTCTDA LKRSMPGRII
     GVSVDARGNK AYRLSLQTRE QHIRREKANS NVCTAQALLA VMASMYGVFH GPDGLKAIAQ
     TVHRKTARMA DGLTELGFKV DPQDYFDTIT VKVGSMQGVI LAAALREGVN LRKVGTDRIG
     ITLDELTLGR TIEAVWRAFG AEGMVYDKTR MVYHLPQEML RESSYMTHPI FHMNRAEAEM
     TRYMRRLADR DLALDRAMIP LGSCTMKLNA TVEMLPLTWP EFANLHPFAP ADQAAGYHEM
     IAELSQMLCD VTGYDAMSMQ PNSGAQGEYA GLLAIRGYHR ARGEGHRNIC LIPTSAHGTN
     PASAQMVGWK VVVVKSAENG DIDLEDFRAK AEQHSENLAG CMITYPSTHG VFEEIVREVC
     DITHAHGGQV YIDGANMNAM VGLSAPGDLG GDVSHLNLHK TFCIPHGGGG PGMGPIGVKA
     HLAPHLPSHA TATGAGFGDA GAVASAAYGS PSILTISYAY CLLMGGAGLT QATKVAILNA
     NYMAKRLSAG FPILYANDKG RVAHECILDT RVLDKIAGVT VEDVAKRLMD CGFHAPTMSW
     PVAGTLMVEP TESEPKAELD RFCDAMLAIR EEADAIAAGS LDAENNPLKR APHTVEDLVG
     DWDRPYSREQ ACYPPGAFRV DKYWPPVNRV DNAYGDRNLV CTCPPVEDYA EPAE