ID   GCSP_GLUOX              Reviewed;         951 AA.
AC   Q5FRY0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 106.
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=GOX1097;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(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=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; CP000009; AAW60866.1; -; Genomic_DNA.
DR   RefSeq; WP_011252658.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FRY0; -.
DR   SMR; Q5FRY0; -.
DR   STRING; 290633.GOX1097; -.
DR   KEGG; gox:GOX1097; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_5; -.
DR   Proteomes; UP000006375; 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:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 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..951
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227105"
FT   MOD_RES         709
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   951 AA;  101236 MW;  66D2E6842A394192 CRC64;
     MPENLPVTTL WPAQTEDFSS RHIGPRPSEI GEMLRVVGAS SLDDLIDKTI PAAILDRGDH
     GIGAALTEQD ALARLRQIAS RNQVLTSMIG QGYYDTVLPP VIQRNILENP AWYTAYTPYQ
     PEISQGRLEA LLNFQTLVAD LTGLDIANAS LLDEGTACAE AMALAQRVGK SKATAFFVDA
     DTHPQTIAVI RTRAEPLGWD VVVGDPETDL DASSVFGALL SYPGSSGQVR DPRKVIAALH
     EKGAIAALAC DPLALVLLES PGALGADIAI GSMQRYGVPM GAGGPHAAFM ATRDAFKRHM
     PGRLVGVSRD SAGKPAYRLA LQTREQHIRR EKATSNICTA QALLAIIASM YAVYHGPEGL
     KAIAARTHRM AAILSAGLKT LGATVETDVF FDTITVQAGA SAPQVLARAV ASGINLRDAG
     DGRIGMSCDE TTTPETIRAV WAAFAGEGAD LSAIEQALDV ADALPEGLSR TAPLLTHPVF
     HAHRSETDLL RYMRALADKD LALDRTMIPL GSCTMKLNAT AEMIPITWPE FARIHPFAPA
     DQVQGYTELF AYLERTLCAI SGYDAVSLQP NSGAQGEYAG LLAIRGYHRA RGDENRDVCL
     IPASAHGTNP ASAQMAGMRV VVVACDENGN VDVEDLKAKI AQHDGRVAAI MITYPSTHGV
     FEERIVEICE LVHAAGGQVY LDGANLNAQV GLARPGLYGA DVSHFNLHKT FCIPHGGGGP
     GMGPIGVGKH LAPYLPGRHG IAVSAAPFGS ASILPISAAY IMMMGDEGLR QATTMAILNA
     NYIASRLEGH YPVLYRGTNG FTAHECIVDL RSLKDAVGVT VDDIAKRLID HGFHAPTVSF
     PVAGTFMIEP TESEGKGELD RFCDAMIAIR AEIAEVEAGR VGMEDSPLRF APHTTADLAG
     DWERSYSREA GCFPGGVDTA KYWSPVGRLD NAWGDRNLVC SCPDISTYVE G
//