ID   GCSP_NITWN              Reviewed;         954 AA.
AC   Q3ST46;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 107.
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=Nwi_1284;
OS   Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS   NCIMB 11846 / Nb-255).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Nitrobacter.
OX   NCBI_TaxID=323098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255;
RX   PubMed=16517654; DOI=10.1128/aem.72.3.2050-2063.2006;
RA   Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA   Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA   Hickey W.J.;
RT   "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT   Nitrobacter winogradskyi Nb-255.";
RL   Appl. Environ. Microbiol. 72:2050-2063(2006).
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; CP000115; ABA04545.1; -; Genomic_DNA.
DR   RefSeq; WP_011314571.1; NC_007406.1.
DR   AlphaFoldDB; Q3ST46; -.
DR   SMR; Q3ST46; -.
DR   STRING; 323098.Nwi_1284; -.
DR   EnsemblBacteria; ABA04545; ABA04545; Nwi_1284.
DR   KEGG; nwi:Nwi_1284; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_5; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000002531; 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..954
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227109"
FT   MOD_RES         699
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   954 AA;  102794 MW;  24D9EE73A28C9B9A CRC64;
     MIAREEPATT FARRHIGPSS RDIAAMLETV GAKSLEALMN EALPPSIRQK TPLDLGEGFS
     ETEVLTHMQA LAAQNQPLTS LIGQGYSGTI LPAVIQRNIL ENPAWYTAYT PYQPEISQGR
     LEALFNFQTM ICDLTGLDVA NASLLDEATA AAEAMALAER ASSVKTKAFF VDHEVHPQTL
     AVLRTRAEPL GWTLVTGDPL HDLDKADVFG AVLQYPGTSG VVRDLRPAIA AIKAKGGLAV
     VAADLLALTL LTSPGVLGAD IAIGSAQRFG VPMGYGGPHA AYMAVCNALK RLLPGRLVGL
     SVDSRGTPAY RLALQTREQH IRREKATSNI CTAQVLLAVI SSMYAVYHGP EGLAQIARTV
     HRHTATLAAG LTRLGFAPLN STAFDTLTVN AGERQSEIVK RASSQGINLR INADGTLGIA
     LDELTIEETV EALWRAFGAT WSYADVEAHA PDLLPADLKR KTAYLTHPVF HEHRSETELL
     RYMRKLSDRD LALDRAMIPL GSCTMKLNAT TEMIPLTWAA FANLHPFAPP EQAEGYFTLF
     ENFEEWLLDI TGYDAISLQP NSGAQGEYAG LLAIRGYHAA RGESHRTVCL IPSSAHGTNP
     ASANMAGMDV VVVACDARGD VDVDDLRTKS TQHADRLAAI MITYPSTHGV FEERIREICD
     IVHGHGGQVY LDGANMNAQV GLSRPGDYGA DVSHLNLHKT FCIPHGGGGP GMGPIGVKAH
     LAPFLPGHPA IDDATPSAVG PVSAAPFGSA SILTISYIYI LMMGSEGLKR ATEVAILNAN
     YIAQRLDPHF PVLYRNVKGR VAHECIIDPR ALKAKTGVTV DDIAKRLIDY GFHAPTMSFP
     VPGTLMIEPT ESESKAELDR FCDAMIAIRQ EIAEIEAGRW KVEASPLRHA PHTAHDIADD
     AWSRPYSRAQ GCFPSGSSRS DKYWCPVGRV DNAYGDRNLV CSCPPVEDYA QAAE