GCSP_SHEON
ID GCSP_SHEON Reviewed; 962 AA.
AC Q8EIQ6;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=SO_0781;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN53857.1; -; Genomic_DNA.
DR RefSeq; NP_716412.1; NC_004347.2.
DR RefSeq; WP_011071084.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EIQ6; -.
DR SMR; Q8EIQ6; -.
DR STRING; 211586.SO_0781; -.
DR PaxDb; Q8EIQ6; -.
DR KEGG; son:SO_0781; -.
DR PATRIC; fig|211586.12.peg.751; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_1_1_6; -.
DR OMA; CVPMSEY; -.
DR OrthoDB; 70707at2; -.
DR PhylomeDB; Q8EIQ6; -.
DR BioCyc; SONE211586:G1GMP-733-MON; -.
DR Proteomes; UP000008186; Chromosome.
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; -; 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..962
FT /note="Glycine dehydrogenase (decarboxylating)"
FT /id="PRO_0000166936"
FT MOD_RES 709
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ SEQUENCE 962 AA; 104673 MW; F5F66632ADD77412 CRC64;
MTKQTLTQLE QHDLFLRRHI GPDSSQQQEM LNYVGAESLD DLTAQIVPES IRLSQELSIG
DSCGEAEGIA YIRGLAKQNQ VFKSYIGMGY YGTQVPNVIL RNVLENPGWY TAYTPYQPEI
AQGRLEAILN FQQVSMDLTG LDLASASLLD EATAAAEAMA LAKRVSKAKK ANIFFVADDV
FPQTLDVVKT RAECFGFEVV VGPASEAVNH ELFGALFQYS NRFGQITDFT DLFAELRAKN
VIVTVAADIM SLVLLKSPGS MGADVVFGSA QRFGVPMGFG GPHAAFFVAR DEHKRSMPGR
IIGVSKDTRG NRALRMAMQT REQHIRREKA NSNICTAQIL LANMASFYAV FHGPQGLKTI
ASRINRFADI LAAGLQAKGV SLVNNTWFDT ISIKGLDVAA VNARALAAEM NLRFDADGIV
GVSLDETTIR TDIDALFEVI LGAGHGLDVA ALDAQIVAQG SQSIPASLVR EDAILSHPTF
NRYQSETEMM RYIKRLESKD LALNYSMISL GSCTMKLNAA VEMIPVSWPE FANMHPFCPL
DQAKGYTQLI EELSSWLVNV TGYDAVCIQP NSGAQGEYAG LLAIRKYHES RGEAHRNICL
IPQSAHGTNP ASAQLAGMQV VVTACDKQGN VDLEDLKAKA AEVAENLSCI MITYPSTHGV
YEETVREICN IVHQHGGQVY LDGANMNAQV GLTSPGFIGA DVSHLNLHKT FAIPHGGGGP
GMGPIGVKAH LAPFVAGHVV VKPGRESDNN GAVSAAPYGS AGILPISWMY IKLLGSKGLK
KSTQTALLNA NYVMKKLSEH YPVLFRGRND RVAHECIIDL RPIKEASGVT EMDIAKRLND
YGFHAPTMSF PVAGTLMIEP TESESKVELD RFIDAMVSIR AEIAKVEAGE WPADNNPLHN
APHTMADIMD SAFDSRPYSR EVAVFPSAAV RTNKFWPTVN RIDDVYGDRN LFCACVPLSD
YE
