ID   GCSP_ROSDO              Reviewed;         949 AA.
AC   Q16AX0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 100.
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};
GN   OrderedLocusNames=RD1_1225;
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS   (strain OCh 114)) (Roseobacter denitrificans).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33942 / OCh 114;
RX   PubMed=17098896; DOI=10.1128/jb.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA   Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA   O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA   Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(2007).
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=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; 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; CP000362; ABG30873.1; -; Genomic_DNA.
DR   RefSeq; WP_011567493.1; NZ_FOOO01000008.1.
DR   AlphaFoldDB; Q16AX0; -.
DR   SMR; Q16AX0; -.
DR   STRING; 375451.RD1_1225; -.
DR   KEGG; rde:RD1_1225; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_5; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000007029; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR003437; GcvP.
DR   InterPro; IPR049316; GDC-P_C.
DR   InterPro; IPR049315; GDC-P_N.
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   NCBIfam; TIGR00461; gcvP; 1.
DR   PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..949
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045604"
FT   MOD_RES         699
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   949 AA;  103442 MW;  10F342B1778B4019 CRC64;
     MSFKPIDYLP YDFANRRHIG PSPAEMTQML EVTGAANLDA LMDDTLPAAI RQKEPLAFGK
     AMSEREVLEH LRRVASKNQV LTSLIGQGYY GTVTPPAIQR NILENPAWYT AYTPYQPEIS
     QGRLEALLNF QTMVSDLTGL EVANASLLDE ATACAEAMTM AQRVSKSKSK AFFVDRDCHP
     QNIAVMQTRA APLGIEIIVG NPDKMDAEAV FGAIFQYPGT YGHVNDFTDH MAALHAHKAI
     GIVSADPLAL TLLKEPGAMG ADIAVGSTQR FGVPEGYGGP HAAYMACRDA YKRAMPGRIV
     GVSVDSHGHR AYRLSLQTRE QHIRREKATS NVCTAQALLA VMASMYAVFH GPEGLRAIAQ
     RIHRKAVRLA KGLEEAGFTV DPQAFFDTIT VDVGPLQAAV MKSAVDEGIN LRRVGETRVG
     ISLNERCRPD TLEAVWRAFG ITRADNDFRP DYRFPEEMLR TSDYLTHPIF HMNRAETEMM
     RYMRRLSDRD LALDRAMIPL GSCTMKLNSA AEMMPVSWRD FSLLHPFAPV DQAKGYTEMI
     DDLSAKLCQI TGYDQISMQP NSGAQGEYAG LLSIAGYHRA NGEAHRNICL IPMSAHGTNP
     ASAQMVGWTV VPIKSADNGD IDMADFAAKA EQHAANLAGC MITYPSTHGV FEETVTEVTR
     ITHQHGGQVY IDGANMNAMV GLSRPGDLGG DVSHLNLHKT FCIPHGGGGP GMGPIGVKSH
     LAPFLPGHEM TGGGEGAVSA APFGSPSLLP ISWAYCLMMG GDGLTQATRV AILNANYIAK
     RLEGAFDVLY RGPTGRVAHE CVIDVRPFEK SAGVSVEDIA KRLIDCGFHA PTMSWPVAGT
     LMVEPTESET KAELDRFCDA MLAIRAEIAD IEEGRMDAAN NPLKNAPHTV DDLVSDWDRP
     YSRDQGCFPP GAFRVDKYWP PVNRVDNVFG DRHLVCTCPP MEDYAEAAE
//