GCSPA_FRATW
ID GCSPA_FRATW Reviewed; 455 AA.
AC A4IZK6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine cleavage system P-protein subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine decarboxylase subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
GN Name=gcvPA {ECO:0000255|HAMAP-Rule:MF_00712}; OrderedLocusNames=FTW_1664;
OS Francisella tularensis subsp. tularensis (strain WY96-3418).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=418136;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WY96-3418;
RX PubMed=17895988; DOI=10.1371/journal.pone.0000947;
RA Beckstrom-Sternberg S.M., Auerbach R.K., Godbole S., Pearson J.V.,
RA Beckstrom-Sternberg J.S., Deng Z., Munk C., Kubota K., Zhou Y., Bruce D.,
RA Noronha J., Scheuermann R.H., Wang A., Wei X., Wang J., Hao J.,
RA Wagner D.M., Brettin T.S., Brown N., Gilna P., Keim P.S.;
RT "Complete genomic characterization of a pathogenic A.II strain of
RT Francisella tularensis subspecies tularensis.";
RL PLoS ONE 2:E947-E947(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_00712}.
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_00712};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. In this organism, the P 'protein' is a heterodimer of two
CC subunits. {ECO:0000255|HAMAP-Rule:MF_00712}.
CC -!- SIMILARITY: Belongs to the GcvP family. N-terminal subunit subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00712}.
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DR EMBL; CP000608; ABO47356.1; -; Genomic_DNA.
DR RefSeq; WP_003020123.1; NC_009257.1.
DR AlphaFoldDB; A4IZK6; -.
DR SMR; A4IZK6; -.
DR KEGG; ftw:FTW_1664; -.
DR HOGENOM; CLU_004620_0_2_6; -.
DR OMA; MYDGASA; -.
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 GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR CDD; cd00613; GDC-P; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00712; GcvPA; 1.
DR InterPro; IPR023010; GcvPA.
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; PTHR42806; PTHR42806; 1.
DR Pfam; PF02347; GDC-P; 1.
DR PIRSF; PIRSF006815; GcvPA; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW Oxidoreductase.
FT CHAIN 1..455
FT /note="Probable glycine dehydrogenase (decarboxylating)
FT subunit 1"
FT /id="PRO_1000045655"
SQ SEQUENCE 455 AA; 49699 MW; 0196338700D98186 CRC64;
MSFIPHKLEQ IKKMLDTIGA SSVDQLFDEI PRHLRADTLK IKDGINEIQL ANLMRKRANK
NHHNINYIGA GAYSHHIPAA IWDIVARGEF YTAYTPYQAE ASQGGLQVIY EFQTMMAGLT
GMDASNASMY DGATALAESV LMAIRSNKKA KSQKVLIAEA LHPTYLRVLE TITKHQGIEF
DIVNLDSKNG KTDVTKLEDF ANTNYAAVVI QSPNFLGQLA DVDGITNWAH KHGALVIAVT
NPMSLAILKS PAEWGDNGAD IVCGEGQPMG VPLASGGPYF GFMTCKMAHV RQMPGRIVGR
TVDLDGNEGF CLTLQAREQH IRRAKATSNI CTNQGLMVTA ATIYMSLLGA EGLERVASIS
HENTQTLATE LAKINGVSIR FNSAFFNEVV IDLPVNAETF VTEMEKEAID AGYFLGEYHS
DLANSIMVCA TEIHTSEDIK EYIEATKKVL ARIGG