ID   GCSP_THEVB              Reviewed;         954 AA.
AC   Q8DII3;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=tll1603;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
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}.
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DR   EMBL; BA000039; BAC09155.1; -; Genomic_DNA.
DR   RefSeq; NP_682393.1; NC_004113.1.
DR   RefSeq; WP_011057442.1; NC_004113.1.
DR   AlphaFoldDB; Q8DII3; -.
DR   SMR; Q8DII3; -.
DR   STRING; 197221.22295328; -.
DR   PRIDE; Q8DII3; -.
DR   EnsemblBacteria; BAC09155; BAC09155; BAC09155.
DR   KEGG; tel:tll1603; -.
DR   PATRIC; fig|197221.4.peg.1682; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000000440; 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; Reference proteome.
FT   CHAIN           1..954
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166940"
FT   MOD_RES         706
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   954 AA;  103795 MW;  014E250CBE6ACF95 CRC64;
     MMVSSPPQLE INLETDAEFV ARHIGITPSD LPKMLSLLGY GSLKELINAV IPPEIRLQRP
     LALSEGLSET AALQKLRTLA QQNQVWRSYI GMGYYNCITP SVIQRNILEN PGWYTQYTPY
     QAEIAQGRLE ALLNFQTLVS DLTGLAIANA SLLDEATAAA EAMTLSFNAC RQRGANRFLV
     AQDCHPQTLA VLRTRALPLG IQIVPIDPIA GELPWENAFG LLLQYPASDG AVRSPQALIA
     AAHERGLLVT VATDLLALTL LRPPGELGAD IAVGSSQRFG VPLGYGGPHA AFFATREDFK
     RQLPGRLVGV SHDALGQRAL RLALQTREQH IRREKATSNI CTAQVLLAVV ASMYAVYHGP
     DGLRQIAERI HQRTVRLAAG LEAAGYQLYY SEFFDTLRIG LGNLPVPVLK ERAAAARINL
     RYFDDGSAGI SLDETTTEKD VADLLALFGA RPAEVEGGDR LPAALKRQSP YLQHPVFQDY
     HSEHALLRYI HRLQAKDLSL TTSMIPLGSC TMKLNATAEM LPISWPEFNQ LHPFAPQEQA
     QGYQALFREL AAMLAEITGF DAISLQPNAG SQGEYAGLLV IRQYHHSRGE SQRNVCLIPT
     SAHGTNPASA VMAGMQVVAV NCDAQGNIDV ADLAAKAETY GDRLAALMIT YPSTHGVFET
     GICQICDIIH RYGGQVYMDG ANMNAQVGLC RPGDFGADVC HLNLHKTFCI PHGGGGPGVG
     PIGVKAHLAP FLPTTQVIPQ GSETGPVTAA PWGSASILPI SWMYITLMGG VGLTRATAIA
     ILNANYIAKR LEPYYPVLYK GAHGLVAHEC ILDLRPLKKS AGIEVEDIAK RLMDYGFHAP
     TVSWPVPGTL MIEPTESETK AELDRFCEAM IAIRSEIAEI EAGVSDRQQN PLKNAPHPAL
     MLATEPWPYP YSREVAAYPA PWLREYKFWP AVARIDNAYG DRHLVCTCSM PLTN