ID   GCSPB_TREDE             Reviewed;         482 AA.
AC   P62031;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
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}; OrderedLocusNames=TDE_1624;
OS   Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS   / KCTC 15104).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX   PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA   Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA   Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA   Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA   Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA   Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA   Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA   Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT   "Comparison of the genome of the oral pathogen Treponema denticola with
RT   other spirochete genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
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; AE017226; AAS12141.1; -; Genomic_DNA.
DR   RefSeq; NP_972230.1; NC_002967.9.
DR   RefSeq; WP_002679310.1; NC_002967.9.
DR   AlphaFoldDB; P62031; -.
DR   SMR; P62031; -.
DR   STRING; 243275.TDE_1624; -.
DR   PRIDE; P62031; -.
DR   EnsemblBacteria; AAS12141; AAS12141; TDE_1624.
DR   GeneID; 2740865; -.
DR   KEGG; tde:TDE_1624; -.
DR   PATRIC; fig|243275.7.peg.1552; -.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_5_0_12; -.
DR   OMA; MHINLHK; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000008212; 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; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00713; GcvPB; 1.
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; PF02347; GDC-P; 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_0000167024"
FT   MOD_RES         264
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00713"
SQ   SEQUENCE   482 AA;  53417 MW;  122CC637802FC530 CRC64;
     MSELIFEKSV KGHKFAEAKL TVPEYKLDSK YLRASDAKLP EVSELEFVRH YMELSKRTHG
     VDNGFYPLGS CTMKYNPKLN EEVADLPNFT NIHPLQPEHT MKGCIEAMGD LGKKLGEITG
     MDAFSLQPSA GAHGEFTALL VIRAYHEKRG DHARNKILVP DSAHGTNPAS AAMVGCEIVN
     IPSDKDGNVD IEELKKTVGN DTAALMLTNP NTLGLFETHI KEIAEIVHKA GGLLYYDGAN
     LNAIMGRLRP GDMGYDIVHL NLHKTFSTPH GGGGPGSGPI GCKKFLEEFL PVPVVTGSDG
     SYKLDYNRPD SIGRVRNFYG NFLVFLRAYA YILTLGSEGI RESSGYAVLN ANYLKKKLEK
     EYDVAFDRIC MHEFVLTLEK IKEETGVSAL DIAKGLIDDG IHPPTMYFPL IVHEALMFEP
     TETESKSTLD FTAEVMIKLK KEAYSNPEKL HGYPYTRPIG RVDETKAARE PVLRYKACCC
     CK