GCSP_PSYIN
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 25-MAY-2022, 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}; OrderedLocusNames=Ping_2729;
OS Psychromonas ingrahamii (strain 37).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=357804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=37;
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 Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA Richardson P.;
RT "Complete sequence of Psychromonas ingrahamii 37.";
RL Submitted (JAN-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=(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; 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 EnsemblBacteria; ABM04439; ABM04439; Ping_2729.
DR KEGG; pin:Ping_2729; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_1_1_6; -.
DR OMA; TIDICMT; -.
DR OrthoDB; 70707at2; -.
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; 3.40.640.10; -; 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; 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