ID   GCSP_SHEWM              Reviewed;         969 AA.
AC   B1KG87;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 92.
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};
GN   OrderedLocusNames=Swoo_3967;
OS   Shewanella woodyi (strain ATCC 51908 / MS32).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=392500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51908 / MS32;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella woodyi ATCC 51908.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; 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; CP000961; ACA88224.1; -; Genomic_DNA.
DR   RefSeq; WP_012326554.1; NC_010506.1.
DR   AlphaFoldDB; B1KG87; -.
DR   SMR; B1KG87; -.
DR   STRING; 392500.Swoo_3967; -.
DR   KEGG; swd:Swoo_3967; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   Proteomes; UP000002168; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR003437; GcvP.
DR   InterPro; IPR049316; GDC-P_C.
DR   InterPro; IPR049315; GDC-P_N.
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   NCBIfam; TIGR00461; gcvP; 1.
DR   PANTHER; PTHR11773:SF13; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..969
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000132456"
FT   MOD_RES         716
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   969 AA;  105773 MW;  77986D152BDE4B80 CRC64;
     MTTETLTTLE QHDRFLGRHI GPDSEQRQEM LNYVGAESLE DLTTQIVPES IRLNRDLAVG
     DNVSEAEGLA YIRQIADKNK VFKSYIGMGY YGTEVPSVIQ RNVLENPGWY TAYTPYQPEI
     AQGRLEAILN FQQLSMDLTG LDLASSSLLD EATAAAEAMA LAKRVSKAKK ANIFFVADDV
     FPQTLDVIKT RAECFGMEVV VGPAEEAVNY ELFGALFQYT NRYGQITDFT ELFTALHEKK
     AIISVAADIM SLVMLKSPGS MGADVVFGNS QRFGVPMGFG GPHAAFFVSR DAHKRSLPGR
     IIGVSQDTRG NRALRMAMQT REQHIRREKA NSNICTAQVL LANMASFYAV FHGPQGLKVI
     AERIHRLTDI LAAGLTAKGV ELVNNTWFDT LSIKGLDAKA VQKRADAAGI NLRVDSCSES
     DGSSDQVLGV SLAETTTRTD VTQLFDVILG EGHGLDVAAL DAQVMADSTS VPAELVRQDA
     ILTHPTFNRY HSETEMMRYI KRLENKDLAL NHSMISLGSC TMKLNAATEM MPITWPEFGN
     MHPFCPQDQA QGYAQLLGEL SEWLVDITGY DAVSLQPNSG AQGEYAGLLA IKQYHESRGD
     AHRNICLIPS SAHGTNPASA QLAGMKIVVT ACDKAGNIDM EDLKAKAAEV ADNLSCIMVT
     YPSTHGVYEE TIGEICEVIH QHGGQVYLDG ANMNAQVGLT SPGFIGADVS HLNLHKTFAI
     PHGGGGPGMG PIGVKKHLAP FLSGHSVVKH GLESDGNGAV SAAPYGSAGI LPITWMYIKL
     LGKQGLREST QVALLNANYM MKKLSEHYPV LYTGRNDRVA HECIIDLRPL KEASGVTEMD
     IAKRLNDYGF HAPTMSFPVA GTLMIEPTES ESKVELDRFI EAMVSIRAEA ARVESGEWPV
     DNNPLHNAPH TLADIMDPEF DSRPYSREVA VFPTAAVKQN KFWPTVNRID DVYGDRNLFC
     ACVPISDYE
//