ID   GCSP_SHESW              Reviewed;         962 AA.
AC   A1RFY8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=Sputw3181_0732;
OS   Shewanella sp. (strain W3-18-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=351745;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W3-18-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. W3-18-1.";
RL   Submitted (DEC-2006) 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=(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; CP000503; ABM23583.1; -; Genomic_DNA.
DR   RefSeq; WP_011788113.1; NC_008750.1.
DR   AlphaFoldDB; A1RFY8; -.
DR   SMR; A1RFY8; -.
DR   GeneID; 45043701; -.
DR   KEGG; shw:Sputw3181_0732; -.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000002597; 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.
FT   CHAIN           1..962
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045615"
FT   MOD_RES         709
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   962 AA;  104568 MW;  E10DF94E0B28DCBD CRC64;
     MTKQTLTQLE QHDLFLRRHI GPDSSQQQAM LNYVGAESLD DLTAQIVPES IRLSQELSIG
     DSCGEAEGIA YIRGLAKQNQ VFKSYIGMGY YGTQVPNVIL RNVLENPGWY TAYTPYQPEI
     AQGRLEAILN FQQVSMDLTG LDLASASLLD EATAAAEAMA LAKRVSKAKK ANIFFVADDV
     FPQTLDVVKT RAECFGFEVV VGPASEAVNH ELFGALFQYT NRFGQITDFT ELFAELRAKN
     VIVTVAADIM SLVLLKSPGA MGADVVFGSA QRFGVPMGFG GPHAAFFVAR DEHKRSMPGR
     IIGVSKDARG NRALRMAMQT REQHIRREKA NSNICTAQIL LANMASFYAV FHGPDGLKTI
     ASRIHRFADI LAAGLQAKGV SLVNSTWFDT LSIKGLDVAA VNARALAAEM NLRFDADGTV
     GVSLDETTLR TDIDALFDVI LGAGHGLDVA ALDAQIVAQG SQSIPAALVR QDAILSHPTF
     NRYQSETEMM RYIKRLESKD LALNYSMISL GSCTMKLNAA VEMIPVSWPE FANMHPFCPL
     DQAKGYTQLI EELSSWLVNV TGYDAVCIQP NSGAQGEYAG LLAIKKYHES RGDAHRNICL
     IPQSAHGTNP ASAQLAGMQV VVTACDKQGN VDLEDLKTKA AEVAENLSCI MITYPSTHGV
     YEESIREICD IVHQHGGQVY LDGANMNAQV GLTSPGFIGA DVSHLNLHKT FAIPHGGGGP
     GMGPIGVKSH LAPFVAGHVV VKPGRVSDNN GAVSAAPYGS AGILPISWMY IKLLGSNGLK
     KSTQTALLNA NYVMKKLSEH YPVLFRGRND RVAHECIIDL RPLKEASGVT EMDIAKRLND
     YGFHAPTMSF PVAGTLMIEP TESESKVELD RFIDAMVSIR AEIAKVESGE WPADNNPLHN
     APHTMADIMD PEFDTRPYSR EVAVFPSAAV RTNKFWPTVN RIDDVYGDRN LMCSCAPLSD
     YE