ID   GCSP_PSYIN              Reviewed;         966 AA.
AC   A1SY74;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 100.
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=Ping_2729;
OS   Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17664 / CCUG 51855 / 37;
RX   PubMed=18460197; DOI=10.1186/1471-2164-9-210;
RA   Riley M., Staley J.T., Danchin A., Wang T.Z., Brettin T.S., Hauser L.J.,
RA   Land M.L., Thompson L.S.;
RT   "Genomics of an extreme psychrophile, Psychromonas ingrahamii.";
RL   BMC Genomics 9:210-210(2008).
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; CP000510; ABM04439.1; -; Genomic_DNA.
DR   RefSeq; WP_011770994.1; NC_008709.1.
DR   AlphaFoldDB; A1SY74; -.
DR   SMR; A1SY74; -.
DR   STRING; 357804.Ping_2729; -.
DR   KEGG; pin:Ping_2729; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   OrthoDB; 9801272at2; -.
DR   Proteomes; UP000000639; 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..966
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045597"
FT   MOD_RES         713
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   966 AA;  106258 MW;  DFDCB94018300327 CRC64;
     MTDTTLLDLL SDSKEFATRH NGSGAAQQKK MLETIGVQSI EQLIDQTVPA AIRLPEKMKL
     AEPQSESMTL ASLKAIAEKN IVNRSFIGQG YYNTLLPNVI LRNVLENPGW YTAYTPYQPE
     ISQGRLESLL NYQQMVMDLT AMEIANASLL DEATAAAESM TLCKRAGKSK SLAFFVADGI
     HPQTVDVVRT RAEFFGYEII SGSMEDLDNH DLFGALLQYP STTGNIQDLT AIIEKAHAKK
     TLVSVASDLL ALTLLKAPGE MGADIVIGSA QRFGIPMGFG GPHAGFMATK EKFKRTMPGR
     IIGVSKDSKG KPALRMAMQT REQHIRREKA TSNICTAQAL LANMSAFYAL YHGPEGLRKI
     ARRVHHLTAI LVAGLRSEGF ELANQHFFDT ITLNSNEHSK AIYHRALAEG MNLRKFPTPD
     NMPVQLGISL DETTTITDVE DLLRVITGKA LSSAGFAAQV AEDEFAGIPA TCRRRSKYLT
     HPIFNEHHSE TQMMRYMKKL ENKDYSLTHG MIPLGCCTMK LNAAALMLPV SWPEFSQMHP
     FAPTEQSFGY QELAEKLSKM LCEVTGYDGF SLQPNSGAQG EYAGLIAIHR YHQSNGEDQR
     NICLIPSSAH GTNPATASML SMKVVVVGCD QQGNIDHADL KAKIDKHRDN LSCIMVTYPS
     THGIYEEGIQ EICEWVHEAG GQVYLDGANM NAQIGLTSPG FIGSDVSHLN LHKTFCIPHG
     GGGPGMGPIG VKKHLIPFLP GHIEVTESAD NKHYAVSAAE LGSASILPIS YAYIAMMGEQ
     GLTSATQIAI LNANYIMERL RPHYPILYQG KEGRVAHECI IDIRPLEAAS GISNEDIAKR
     LMDYGFHAPT MSFPVGGTFM IEPTESESTA ELDRFCDAMI AIRHEIKQIE DGEWSATDNP
     LVNAPHTQVD LMESEWTHGY SRELACFPSK HSKDSKYWPT VNRVDNVFGD RNLICSCPSI
     ESYMEE
//