ID   GCSP1_PSEF5             Reviewed;         951 AA.
AC   Q4K7Q8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Glycine dehydrogenase (decarboxylating) 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine decarboxylase 1 {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) 1 {ECO:0000255|HAMAP-Rule:MF_00711};
GN   Name=gcvP1 {ECO:0000255|HAMAP-Rule:MF_00711}; OrderedLocusNames=PFL_4641;
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000076; AAY93888.1; -; Genomic_DNA.
DR   RefSeq; WP_011062895.1; NC_004129.6.
DR   AlphaFoldDB; Q4K7Q8; -.
DR   SMR; Q4K7Q8; -.
DR   STRING; 220664.PFL_4641; -.
DR   EnsemblBacteria; AAY93888; AAY93888; PFL_4641.
DR   KEGG; pfl:PFL_4641; -.
DR   PATRIC; fig|220664.5.peg.4747; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_2_1_6; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000008540; 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..951
FT                   /note="Glycine dehydrogenase (decarboxylating) 1"
FT                   /id="PRO_0000227116"
FT   MOD_RES         703
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   951 AA;  102473 MW;  BBF2ACC0CF69E95F CRC64;
     MTVNLSTANE FIARHIGPRQ GDEQAMLNSL GFDSLEALSA SVIPESIKGT SVLELGHGLS
     EAQALASIKA IAARNQLFKT YIGQGYYNCH TPSPILRNLL ENPAWYTAYT PYQPEISQGR
     LEALLNFQTL ISDLSGLPIA NASLLDEGTA AAEAMTFCKR LSKNKGSHAF FASQHCHPQT
     LDVLRTRAEP LGINVVVGDE RKLTDVSPFF GALLQYPASN GDLFDYRELT ERFHAANALV
     AVAADLLALT LLTPPGEFGA DVAIGSAQRF GVPLGFGGPH AAYFATRDAF KRDMPGRLVG
     VSVDRFGKPA LRLAMQTREQ HIRREKATSN ICTAQVLLAN IASMYAVYHG PKGLTQIAQR
     IHQLTAILAK GLVQLGLTVE QESFFDTLSL HTAGRTAALH DKARAQGINL RVIDAERLGL
     SLDETTTQAD VETLWSLLAD GKPAPDFAAL AAAVTSGIPA ALARQSAILS HPVFNRYHSE
     TELMRYLRKL ADKDLALDRT MIPLGSCTMK LNAASEMIPI TWAEFGALHP FAPAEQSAGY
     QQLTTELEAM LCAATGYDAV SLQPNAGSQG EYAGLLAIRA YHQSRGDERR DICLIPSSAH
     GTNPATANMA GMRVVVTACD ARGNVDIEDL RAKAIEHREH LAALMITYPS THGVFEEGIR
     EICGIIHDNG GQVYIDGANM NAMVGLCAPG KFGGDVSHLN LHKTFCIPHG GGGPGVGPIG
     VKSHLAPFLP GHAALENKKG AVCAAPFGSA SILPITWMYI SMMGGAGLKR ASQLAILNAN
     YISRRLEEHY PVLYTGSNGL VAHECILDLR PLKDSSGISV DDVAKRLIDF GFHAPTMSFP
     VAGTLMIEPT ESESKEELDR FCDAMIRIRE EIRAVENGAL DKDDNPLKNA PHTAAELVGE
     WSHPYSREQA VYPVASLVEG KYWPPVGRVD NVFGDRNLVC ACPSIESYQD A