GCSP_XANAC
ID GCSP_XANAC Reviewed; 977 AA.
AC Q8PN59;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 109.
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=XAC1214;
OS Xanthomonas axonopodis pv. citri (strain 306).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190486;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=306;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(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; AE008923; AAM36086.1; -; Genomic_DNA.
DR RefSeq; WP_011050782.1; NC_003919.1.
DR AlphaFoldDB; Q8PN59; -.
DR SMR; Q8PN59; -.
DR STRING; 190486.XAC1214; -.
DR EnsemblBacteria; AAM36086; AAM36086; XAC1214.
DR KEGG; xac:XAC1214; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_1_1_6; -.
DR OMA; CVPMSEY; -.
DR Proteomes; UP000000576; 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..977
FT /note="Glycine dehydrogenase (decarboxylating)"
FT /id="PRO_0000166948"
FT MOD_RES 702
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ SEQUENCE 977 AA; 104699 MW; 049E8B9B1357535E CRC64;
MSQTPSSLRD LEHHSAFVER HIGPNDAEIA QMLDVVGHAS LDALTDAIVP GNIKSPAPLA
LPEAITEEEA LAKIRAIASK NQVQRNFIGQ GYYGTHTPKV ILRNILENPA WYTAYTPYQA
EISQGRMEAL INFQTLCADL TGMQIANASL LDEATAAAEA MTLAKRSAKS KSNTFFVHDA
VHPQTLELLR TRAEPLDIVL RVGTPEEALQ AECFGVLLQY PDSFGHIGDH AALADAVHAQ
GGLVAVATDL LALTLIAAPG EWGADIVVGN SQRFGVPFGF GGPHAAFMAC RDAYKRSMPG
RLIGVSIDAA GNPAYRLTLQ TREQHIRREK ATSNICTAQV LLAVMASMYA VYHGPDGLVR
IARRTHRLAA ILAAALRSAG VSVGDRFFDT LHVKAIDADA IHARARAAGI NLRAIDSEAV
GISLDETTTR ADVVALAQLF GATADVDALD AATADALPQG LLRTTPFLTH PVFNTHHSEH
ELLRYMRSLA DKDLAMDRTM IPLGSCTMKL NATAEMIPVT WPEFGAIHPL APAEQSAGYA
QLIDELEAML VECTGYDAVS LQPNSGAQGE YAGLLAIRAY HRSRGQAHRD ICLIPESAHG
TNPASAQMCG MTVVVTKCDA NGNVDVDDIR AKAEKYSDRL AALMITYPST HGVFEEDVVA
ICEAVHAHGG QVYTDGANMN ALVGVAKPGK WGSDVSHLNL HKTFCIPHGG GGPGVGPCAV
KSHLAPYLPR AGIHAGEGQT AAIHGGGFNS ESGNGHSSRI GGMVSAAAYG SASILPISWM
YVTMMGSAGL RKATQVALLN ANYIAKRLAP HYKTLYTGRN GLVAHECILD VRPLEKTSGI
GAEDIAKRLI DFGFHAPTLS FPVAGTLMVE PTESESQHEL DRFIDAMIQI REEIRAIEDG
RLDREDNPLK HAPHTATQVS ASEWTHAYPR ELAAFPLPSL KQQKYWPPVA RVDNVYGDKN
VMCACIPVDA YKEDAEA
