GCSP_DEIRA
ID GCSP_DEIRA Reviewed; 949 AA.
AC Q9RTF5;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 115.
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=DR_1809;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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; AE000513; AAF11360.1; -; Genomic_DNA.
DR PIR; E75352; E75352.
DR RefSeq; NP_295532.1; NC_001263.1.
DR RefSeq; WP_010888444.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RTF5; -.
DR SMR; Q9RTF5; -.
DR STRING; 243230.DR_1809; -.
DR PRIDE; Q9RTF5; -.
DR EnsemblBacteria; AAF11360; AAF11360; DR_1809.
DR KEGG; dra:DR_1809; -.
DR PATRIC; fig|243230.17.peg.2021; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_1_1_0; -.
DR InParanoid; Q9RTF5; -.
DR OMA; CVPMSEY; -.
DR OrthoDB; 70707at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR CDD; cd00613; GDC-P; 2.
DR Gene3D; 3.40.640.10; -; 2.
DR Gene3D; 3.90.1150.10; -; 1.
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..949
FT /note="Glycine dehydrogenase (decarboxylating)"
FT /id="PRO_0000166912"
FT MOD_RES 697
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ SEQUENCE 949 AA; 102123 MW; FDCBA42D4E0888D5 CRC64;
MTKSLSDLLQ TNDFTRRHIG PSEAEQAEML GVLGVSSLDE LTQTTLPAAI QFDGELHTGP
GMTEAQALAE LKAVAQKNKV FRSYIGMGYA GTDVPPVILR NMLENPGWYT AYTPYQAEIS
QGRLEMLLNF QQTVQDMTGM PVSNASLLDE ATAAAEAMTL AKRQSKNKGS NVFFVADNVH
PQTMDVVKTR AEYFGFEVQT GSADAIPEGA FGALVQYPGT HGEVLNLAPI AEKAHTQGAA
LIVATDLLAC ALLTPPGEQG ADIVVGSAQR FGVPMGFGGP HAAFLACQKG FERSMPGRVI
GVSKDVRGNT ALRMAMQTRE QHIRREKATS NICTAQALLA NMAAAYAVWH GPEGIKTIAE
RVHRLTGILA KALQDAGIKA NETFFDTLTF EGQDDLGARA EAKGINFRLD GGKVGISLDE
TVTPQDLADI IEVVTGKGVD VQKLDAEAVD GIPAPLKRQS DFLTHPVFNT HHSEHGMLRY
LKQLENKDYS LTHGMIPLGS CTMKLNATTE MIPVTWPEFG GLHPFAPESQ TQGYAEMLAE
LERWLADITG YDAVSMQPNS GAQGEYAGLL VIRKYHEARG EAHRNICLIP ASAHGTNPAS
AAMMGMQVVV VKTDEQGNID FDDLKAQAEA HSDHLAALMI TYPSTHGVYE ENVRDVCDLI
HQHGGQVYLD GANMNAMVGV AKPGLIGGDV SHLNLHKTFA IPHGGGGPGM GPIGVKAHLA
PFLPNHAVAP TSDSHTGAVS AAPYGSASIL PISYLYIKLL GAAGLRQSTQ VALLNANYIA
KRLSGAFPVL YSGKGGRVAH ECILDIRPLK QESGVSEEDI AKRLMDYGFH APTMSFPVPG
TLMIEPTESE PKAELDRFVD AMLNIRREIQ DVQDGTISAA DSPLKHAPHT LKDLMDSEWT
RAYSRETGAF PSAAQKAWKY WPAVNRVDNV YGDRNFVCSC PPIEDYIGA
