ID   GCSP_SERP5              Reviewed;         959 AA.
AC   A8GIR9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
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=Spro_3914;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) 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; CP000826; ABV43009.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8GIR9; -.
DR   SMR; A8GIR9; -.
DR   STRING; 399741.Spro_3914; -.
DR   KEGG; spe:Spro_3914; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   OrthoDB; 9801272at2; -.
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.
FT   CHAIN           1..959
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000062077"
FT   MOD_RES         708
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   959 AA;  104560 MW;  D7874766280630A9 CRC64;
     MTQTLSQLEH SEAFIERHIG SSAQQQQQLL EAVGARSLNA LIQQIVPADI QLPAPPPVGD
     AATEHQALAE LKAIASQNQR YKSYIGMGYS AVLTPPVILR NMLENPGWYT AYTPYQPEVS
     QGRLEALLNF QTVTLDLTGL DLASASLLDE ATAAAEAMAL AKRASKLKDA NRFFVADDVH
     PQTLDVVRTR AATFGFEVIV DKAEKVLELQ GVFGVLLQQV GTTGELHDYS ALLAELKNRK
     IGTSVAADIM ALVLLTAPGK QGADVVFGSA QRFGVPMGYG GPHAAFFACR DEFKRSMPGR
     IIGVSRDAAG NTALRMAMQT REQHIRREKA NSNICTSQVL LANIASLYAV YHGPQGLQRI
     AGRIHRLTDI LAAGLQQAGL QLRHKTWFDT LTVEVKDKAA VLERALSFGI NLRTDIHGAV
     GITLDEATSR EDVQTLFALL AGDNHGLDID ALDAAVSKNS QSIPAGMLRK DPILTHPVFN
     SYHSETEMMR YMHRLERKDL ALNQAMIPLG SCTMKLNAAA EMIPITWPEF SELHPFCPPE
     QAAGYKQMIG QLSQWLVQLT GYDAVCMQPN SGAQGEYAGL LAIRHYHESR NESGRHICLI
     PSSAHGTNPA SAQMAGMSVV VVACDKNGNI DLHDLRVKAE QAGEELSCIM VTYPSTHGVY
     EETIREVCQI VHQFGGQVYL DGANMNAQVG ITTPGYIGAD VSHLNLHKTF CIPHGGGGPG
     MGPIGVKAHL APFVPGHSVV QIDGVLTQQG AVSAAPFGSA SILPISWMYI RMMGAEGLKQ
     ASQVAILNAN YIATRLKDAY PVLYTGRDHR VAHECILDIR PLKEETGISE MDIAKRLIDY
     GFHAPTMSFP VAGTLMVEPT ESESKVELDR FIDAMLAIRS EIDRVAKGEW PLEDNPLVNA
     PHIQAELVSD WQHAYSRELA VFPIAGVREN KYWPSVKRLD DVYGDRNLFC SCVPMSEYE
//