ID   GCSP_NITHX              Reviewed;         958 AA.
AC   Q1QMW0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=Nham_1618;
OS   Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Nitrobacter.
OX   NCBI_TaxID=323097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10229 / NCIMB 13809 / X14;
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA   O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA   Gentry M.E., Bruce D., Richardson P.;
RT   "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL   Submitted (MAR-2006) 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}.
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; CP000319; ABE62437.1; -; Genomic_DNA.
DR   RefSeq; WP_011510122.1; NC_007964.1.
DR   AlphaFoldDB; Q1QMW0; -.
DR   SMR; Q1QMW0; -.
DR   STRING; 323097.Nham_1618; -.
DR   EnsemblBacteria; ABE62437; ABE62437; Nham_1618.
DR   KEGG; nha:Nham_1618; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_5; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000001953; 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..958
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045593"
FT   MOD_RES         703
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   958 AA;  102759 MW;  AAD18BBFE8AD77A1 CRC64;
     MTAREEPATT FARRHIGPSS RDIAAMLETV GAKSLAALMN EALPPSIRQA APLDLGQGLS
     EGLSETEALA HMQSLAAQNQ AFTSLIGQGY SGTILPAVIQ RNILENPAWY TAYTPYQPEI
     SQGRLEALFN FQTMICDLTG LDVANASLLD EATAVAEAMA LAERASSVKT KAFFVDHEVH
     PQTLAVLRTR AEPLGWTLVT GDPLRDLDKA DVFGAVLQYP GTSGVVRDLR PAISTLKAKG
     GLAVVAADLL ALTLLASPGV LGADIAVGSA QRFGVPMGYG GPHAAYMAVR DTLKRLLPGR
     IVGLSVDSRG APAYRLALQT REQHIRREKA TSNICTAQVL LAVISSMYAV YHGPEGLAQI
     ARTVHRRTAT LAAGLTRLGF APLNDAAFDT LTVSVGDRQN EIAGRALSQG INLRINADHT
     LGIALDELTT PEIVEAVWRT FGAAFSYADV EAHAPDLLPA DLGRRTAYLT HPVFHAHRSE
     TELLRYMRKL SDRDLALDRA MIPLGSCTMK LNATTEMIPL TWPAFAGLHP FAPCEQAEGY
     YALFEEFEQW LIDITGYDAI SLQPNSGAQG EYAGLLAIRG YHAARGDSHR TVCLIPSSAH
     GTNPASANMA GMEVVVVACD ARGDVDVDDL RAKAAQHADR LAAIMITYPS THGVFEERIR
     EICDIVHSHG GQVYLDGANM NAQVGLSRPG DYGADVSHLN LHKTFCIPHG GGGPGMGPIG
     VKAHLASFLP GHPATDGATP PAVGAVSAAP FGSASILTIS YIYVLMMGGE GLTRATEVAI
     LNANYVAQRL DPHFPVLYRN VKGRVAHECI IDPRALKAET GVTVDDIAKR LIDYGFHAPT
     MSFPVPGTLM IEPTESESKA ELDRFCDAMI AIRREIAEIE AGRWSVEASP LRHAPHTVHD
     IADDTWSRPY SRAQGCFPAG TSRLDKYWCP VGRVDNAYGD RNLVCSCPPM EDYAQAAE