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GCSPA_AQUAE
ID   GCSPA_AQUAE             Reviewed;         439 AA.
AC   O67193;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 110.
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}; Synonyms=gcsP2;
GN   OrderedLocusNames=aq_1109;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC07143.1; -; Genomic_DNA.
DR   PIR; F70395; F70395.
DR   RefSeq; NP_213757.1; NC_000918.1.
DR   RefSeq; WP_010880695.1; NC_000918.1.
DR   AlphaFoldDB; O67193; -.
DR   SMR; O67193; -.
DR   STRING; 224324.aq_1109; -.
DR   EnsemblBacteria; AAC07143; AAC07143; aq_1109.
DR   KEGG; aae:aq_1109; -.
DR   PATRIC; fig|224324.8.peg.866; -.
DR   eggNOG; COG0403; Bacteria.
DR   HOGENOM; CLU_004620_0_2_0; -.
DR   InParanoid; O67193; -.
DR   OMA; MYDGASA; -.
DR   OrthoDB; 870147at2; -.
DR   Proteomes; UP000000798; 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   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; Reference proteome.
FT   CHAIN           1..439
FT                   /note="Probable glycine dehydrogenase (decarboxylating)
FT                   subunit 1"
FT                   /id="PRO_0000166953"
SQ   SEQUENCE   439 AA;  49722 MW;  88953271141E75EA CRC64;
     MSYIPHSEEE TKEILSKLGL ESLEDLFSHI PKELFAKDFS FPEPKSEEEL RRIFERACED
     TELPLYFIGA GAYDRIIPSV IWQILSRGEF LTPYTPYQAE ASQGTLQAIF EYQSLICELT
     GMDVANASMY DGASALAEAV LMARAIKGKG DTVVLSKALN PLYRRTVKTY LRGYEDKIVE
     VPYTEEGTTD LNNLEEVLKE SEVHALAVQY PNFFGFVEPL KEIGELCKKY EVPFVVFVDP
     IALSILKPPA EFGADIVVGE GQQMGIPLSF GGPYVGFFAT KKEHVRKMPG RLVGMGEDIE
     GKRAFTLVLQ TREQHIRRER ATSNICTNQN LMALANLLYM VLLGKEGMKK VAVQSLSKAL
     YFKKELMKKG FEEVFTGKHL WEFPLRHESL KAIYRKLLKE KIVLGLPLDR FYEDLKNTTL
     IAVTEKRTKE EIDSVLALL
 
 
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