ID   GCSP_SHESH              Reviewed;         962 AA.
AC   A8FZK4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 97.
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=Ssed_3673;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
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., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-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; CP000821; ABV38277.1; -; Genomic_DNA.
DR   RefSeq; WP_012144007.1; NC_009831.1.
DR   AlphaFoldDB; A8FZK4; -.
DR   SMR; A8FZK4; -.
DR   STRING; 425104.Ssed_3673; -.
DR   KEGG; sse:Ssed_3673; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_2_1_6; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000002015; 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..962
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000083216"
FT   MOD_RES         709
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   962 AA;  104778 MW;  F1195EA8A91A8E2F CRC64;
     MTTETLTQLE QHELFIRRHI GPDSAQQQEM LNFVGAESLE DLTQQIVPES IRLNRDLAVG
     SACGEAEGMA YIREIADKNK VFKSYIGMGY YGTEVPSVIQ RNVLENPGWY TAYTPYQPEI
     AQGRLEAILN FQQVSMDLTG LDLASASLLD EATAAAEAMA LAKRVSKAKK ANIFFVADDV
     FPQTLDVVKT RAECFGFEIV VGPASEAVNY ELFGALFQYT NRFGEITDFT ELFTELKAKK
     AVVSVAADIM SLVMLKSPGS MGADVVFGSA QRFGVPMGLG GPHAAFFVTR DAHKRSLPGR
     IIGVSQDTRG NRALRMAMQT REQHIRREKA NSNICTAQVL LANMASFYAV YHGPQGLKII
     AERIHRLTDI LASGLTAKGV ELVNGTWFDT LSLKATDSEA ITARAVAAGI NLRIDSDGVL
     GVSLAETTLR EDIAELFDVI LGEGHGLDVA ALDAEIIKAG SSSIPAQLVR TDAILTHPTF
     NSYHSETEMM RYIKRLENKD LALNHSMISL GSCTMKLNAA TEMMPISWPE FGNMHPFCPL
     DQSEGYTDLI EELSTWLVDI TGYDAMCMQA NSGASGEYAG LLAIRNYHIS RGDAHRNVCL
     IPQSAHGTNP ASAQMAGMKI VVTACDKAGN VDMEDLKAKA AEVAENLSCI MITYPSTHGV
     YEETVSEICE VIHQHGGQVY LDGANMNAQV GLTTPGSIGA DVSHLNLHKT FAIPHGGGGP
     GMGPIGVKAH LAPFVAGHVV VKHGRESDNN GAVSAAPYGS ASILPITWMY IKLLGHQGLR
     QSTQVALLNA NYVMKKLSEH YPVLYTGRNE RVAHECIIDL RPLKESSGVT EMDIAKRLND
     YGFHAPTMSF PVAGTLMIEP TESESKVELD RFIEAMISIR GEASRVESGE WPADNNPLHN
     APHTLADIMD PEFDSRPYSR EVAVFPTAAV KLNKFWPTVN RIDDVFGDRN LFCACVPMSE
     YE
//