GCSP_XANC5
ID GCSP_XANC5 Reviewed; 954 AA.
AC Q3BW89;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
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=XCV1243;
OS Xanthomonas campestris pv. vesicatoria (strain 85-10).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=316273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=85-10;
RX PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005;
RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D.,
RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C.,
RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H.,
RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S.,
RA Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D.,
RA Kaiser O.;
RT "Insights into genome plasticity and pathogenicity of the plant pathogenic
RT Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete
RT genome sequence.";
RL J. Bacteriol. 187:7254-7266(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM039952; CAJ22874.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3BW89; -.
DR SMR; Q3BW89; -.
DR STRING; 456327.BJD11_16410; -.
DR EnsemblBacteria; CAJ22874; CAJ22874; XCV1243.
DR KEGG; xcv:XCV1243; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_3_2_6; -.
DR OMA; CVPMSEY; -.
DR Proteomes; UP000007069; 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..954
FT /note="Glycine dehydrogenase (decarboxylating)"
FT /id="PRO_1000045626"
FT MOD_RES 702
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ SEQUENCE 954 AA; 102578 MW; 17303C000C2FAECC CRC64;
MSQTPSSLRD LEHHSAFVER HIGPNDAEIA QMLDVVGHAC LDALTDAIVP GNIKSPAPLA
LPEAITEEEA LAKIRAIADK NTVFRNFIGQ GYYGTHTPKV ILRNILENPA WYTAYTPYQA
EISQGRMEAL INFQTLCADL TGMQIANASL LDEATAAAEA MTLAKRSAKS RSNTFFVHDA
VHPQTLELLR TRAEPLDIVL RVGTPEEALQ AECFGVLLQY PDSFGHIGDH AALADAVHAQ
GGLVAVATDL LALTLIAAPG EWGADIVVGN SQRFGVPFGF GGPHAAFMAC RDAYKRSMPG
RLIGVSIDAA GNPAYRLTLQ TREQHIRREK ATSNICTAQV LLAVMASMYA VYHGPDGLTR
IARRTHRLAA ILAAALRSAG VTVGERFFDT LHVKAIDANA IHARARAAGI NLRAIDSEAV
GISLDETSTR ADVVALAALF GAQADVDALD AATADALPQG LLRTTPFLTH PVFNTHHSEH
ELLRYMRSLA DKDLAMDRTM IPLGSCTMKL NATAEMIPVT WPEFGAIHPL APAEQSAGYA
QLIDELEAML VECTGYDAVS LQPNSGAQGE YAGLLAIRAY HRSRGEAHRD ICLIPESAHG
TNPASAQMCG MTVVVTKCDA NGNVDVDDIR AKAEKYSDRL AALMITYPST HGVFEEDVVA
ICEAVHAHGG QVYTDGANMN ALVGVAKPGK WGSDVSHLNL HKTFCIPHGG GGPGVGPCAV
KSHLAPYLPK TLGGEGDVGM VSAASYGSAS ILPISWMYVT MMGSAGLRKA TQVALLNANY
IAKRLAPHYK TLYTGRNGLV AHECILDVRP LEKTSGIGAE DIAKRLIDFG FHAPTLSFPV
AGTLMVEPTE SESQHELDRF IDAMIQIREE IRAIEDGRLD REDNPLKHAP HTATQVSASE
WTHAYPRELA AFPLPSLKQQ KYWPPVARVD NVYGDKNVMC ACIPVDAYKE DVEA