ID   GCSPB_AQUAE             Reviewed;         482 AA.
AC   O67740;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE            EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine cleavage system P-protein subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine decarboxylase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
GN   Name=gcvPB {ECO:0000255|HAMAP-Rule:MF_00713}; Synonyms=gcsP1;
GN   OrderedLocusNames=aq_1903;
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_00713}.
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_00713};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00713};
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_00713}.
CC   -!- SIMILARITY: Belongs to the GcvP family. C-terminal subunit subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00713}.
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DR   EMBL; AE000657; AAC07701.1; -; Genomic_DNA.
DR   PIR; H70463; H70463.
DR   RefSeq; NP_214308.1; NC_000918.1.
DR   RefSeq; WP_010881244.1; NC_000918.1.
DR   AlphaFoldDB; O67740; -.
DR   SMR; O67740; -.
DR   STRING; 224324.aq_1903; -.
DR   PRIDE; O67740; -.
DR   EnsemblBacteria; AAC07701; AAC07701; aq_1903.
DR   KEGG; aae:aq_1903; -.
DR   PATRIC; fig|224324.8.peg.1474; -.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_5_0_0; -.
DR   InParanoid; O67740; -.
DR   OMA; MHINLHK; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000000798; 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; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00713; GcvPB; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR023012; GcvPB.
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; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..482
FT                   /note="Probable glycine dehydrogenase (decarboxylating)
FT                   subunit 2"
FT                   /id="PRO_0000166993"
FT   MOD_RES         267
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00713"
SQ   SEQUENCE   482 AA;  54973 MW;  D4D2BE9C407992EE CRC64;
     MELIFEKSKK GRKGYKLPEL DVEEVNIKEY LPEEYLREEL DFPEVSELDV VRHYTNLSHL
     NYAVDTTMVP LGSCTMKYNP RINEELVNKK EFLNVHPLTP EEYIQPLLKL VYELKELLKE
     LGGFAEVSLQ PAAGAHGELL GLLLIHAYHQ DRGNKEKKVV LIPDSAHGTN PASAAICGFD
     IKVVKSDKKG ELDFEDFIKK LDERVAALMI TNPNTLGIFE RKIKEIAEEL HKRDALLYMD
     GANFNALVGR FKPGEWGVDV MHFNLHKTFS TPHGGGGPGA GPVGVSERLK PYLPVPQIEY
     DGKKYYLNWN IEKSVGKILA FHGHFLVWLK ALAYILTYGK DIKKVSEYAV LNARYLKHLL
     KGVFKDPYPE SPCMHEFVLS ATNLTKYGVR ASDVAKRILD YGFYAPTMYF PLIVREALMI
     EPTETENPDT LKKFALILRK IVKEAKEKPE ILKKAPHRTP VRRIKEAEAN RNLILKFKDI
     KE