ID   GCSP_TERTT              Reviewed;         961 AA.
AC   C5BNY8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=TERTU_0724;
OS   Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Teredinibacter.
OX   NCBI_TaxID=377629;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39867 / T7901;
RX   PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA   Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA   Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA   Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA   Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA   Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA   Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA   Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT   "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT   endosymbiont of marine wood-boring bivalves (shipworms).";
RL   PLoS ONE 4:E6085-E6085(2009).
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; CP001614; ACR13967.1; -; Genomic_DNA.
DR   RefSeq; WP_015820082.1; NC_012997.1.
DR   AlphaFoldDB; C5BNY8; -.
DR   SMR; C5BNY8; -.
DR   STRING; 377629.TERTU_0724; -.
DR   EnsemblBacteria; ACR13967; ACR13967; TERTU_0724.
DR   KEGG; ttu:TERTU_0724; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   OMA; DEHCHPQ; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000009080; 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..961
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000212657"
FT   MOD_RES         709
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   961 AA;  105239 MW;  4F241C8877C56485 CRC64;
     MPNTDSLNNL FASDEFISRH IGPDQNQVEK MLATLEVDSL DALIEKTVPA TIREAQPLPL
     AEPVAEHTAL EELKSLAAKN DVFTSYIGLG YHPTRVPNVI LRNVLENPGW YTAYTPYQPE
     IAQGRLEGLL NFQQMITDLT GMEMANASML DEATAAAEAM AMAKRVGRKN SSNCFFIDKN
     CYPQTIAVMR TRAEHFGFDI IVDAPEKALA GEDYFGAILQ YPGADGGIGD IESWIKTIQS
     KDALAIVAAD IMSLVLLRSP GDMGADIVIG CNQRFGIPMG FGGPHAAFFA FKEKHKRSTP
     GRIIGVSVDS RGKQALRMAM QTREQHIRRE KANSNICTSQ VLLAVMSAFY AMYHGAEGVD
     RIARRIHILT KMLSEGLISL GYKLRHTTFF DTLCIEVGDQ QKPLLDRAQH ARINLCAMGS
     GALSISLSEC TTLDDLTALI AVFAGGESPL DMPSLEAKAQ QKAVLSENLL RDGRALQHEI
     FSQYHSETEM LRYLKRLESR DIALNHAMIP LGSCTMKLNA TAEMIPVTWP EFGNMHPFAP
     ISQAAGYAEM FNQLQHMLAA CTGYDAISLQ PNAGSQGEYA GLLTIKKYFE AKGEVRSICL
     IPQSAHGTNP ASAQMASMKV VVVNCDDDGN VDIADLDAKI AQHGENIAAI MVTYPSTHGV
     FEENITQICD KIHAVGAQVY IDGANMNALV GIASPGHFGG DVSHLNLHKT FCIPHGGGGP
     GMGPIGVKDH LAPYLAAHPL QEIPGTVAAN GTVSAAPWGS ASILPISWMY IRMMGAKGMK
     MASEYAILNA NYIAKRLKNH FPILYSGKHG FVAHECLLDL RPLKEASGVS EEDIAKRLMD
     FGFHAPTMSF PVAGTLMIEP TESENQFELD RFCDAMIQIR EEIRKIEQGE LPADDNPLVN
     APHTLDDVCN SEWNRSYTRD QACRPLDYLK HHKVWPTVNR IDNVYGDRNL ICSCPGVDDY
     R