ID   GCSP_SHEPA              Reviewed;         962 AA.
AC   A8H7S9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, 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=Spea_3301;
OS   Shewanella pealeana (strain ATCC 700345 / ANG-SQ1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=398579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700345 / ANG-SQ1;
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.Z., Manno D., Hawari J., Richardson P.;
RT   "Complete sequence of Shewanella pealeana ATCC 700345.";
RL   Submitted (OCT-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; CP000851; ABV88616.1; -; Genomic_DNA.
DR   RefSeq; WP_012156515.1; NC_009901.1.
DR   AlphaFoldDB; A8H7S9; -.
DR   SMR; A8H7S9; -.
DR   STRING; 398579.Spea_3301; -.
DR   KEGG; spl:Spea_3301; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000002608; 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_1000083215"
FT   MOD_RES         709
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   962 AA;  104430 MW;  25BD24D85912E0FD CRC64;
     MTTETLTQLE QHELFLRRHI GPGADQQQEM LNFVGAESLE DLTAQIVPGA ILLNRDLAVG
     DSCGEAEGLA YIRKIADKNK VFKSYIGMGY HGTEVPSVIQ RNVLENPGWY TAYTPYQPEI
     AQGRLEAILN FQQVSMDLTG LDLASSSLLD EATAAAEAMA LSKRVSKAKK ANIFFVADDV
     FPQTIDVIKT RAECFGFEVV VGPAEEAVNY ELFGALFQYT NRVGQICDHT ELFAKLHEKK
     ALVSVAADIM SLVVLKSPGS MGADVVLGNS QRFGVPMGFG GPHAAFFVTR DEYKRSLPGR
     IIGVSQDTRG NRALRMAMQT REQHIRREKA NSNICTAQVL LANMASFYAV FHGPQGLKVI
     AERIHRLTDI VAAALTAKGV ELVNNTWFDT LSIKGLDVTA VQARALATGL NLRIDSDGVI
     GVSLSETTTR SDVAELFDVL LGEGHGQDAA ALDAAIIANG SSSIPSELVR KDAILTHPTF
     NRYQSETEMM RYIKRLENKD LALNHSMISL GSCTMKLNAA TEMAPITWPE FGNMHPFCPQ
     DQAQGYAQLL EELSTWLVDI TGYDAVSLQP NSGAQGEYAG LLAIKQYHES RGDAHRNICL
     IPQSAHGTNP ASAQLAGMKI VVTACDKAGN IDMADLKAKA AEVADNLSCI MVTYPSTHGV
     YEETIGEICE VIHQHGGQVY LDGANMNAQV GLTSPGFIGA DVSHLNLHKT FAIPHGGGGP
     GMGPIGVKKH LAPFLSGHSV VKHGLESDNN GAVSAAPFGS AGILPITWMY IKLLGKKGLR
     QSTQVALLNA NYVMKKLSAH YPVLYTGRND RVAHECIIDL RPLKEASGVT EMDIAKRLND
     YGFHAPTMSF PVAGTLMIEP TESESKVELD RFIEAMVSIR GEIAKVEAGE WPVDNNPLHN
     APHTLADIMD PAFDSRPYSR EEAVFPTNAV KANKFWPTVN RIDDVYGDRN LMCSCAPVSD
     YE
//