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Database: UniProt
Entry: A4IQV3_GEOTN
LinkDB: A4IQV3_GEOTN
Original site: A4IQV3_GEOTN 
ID   A4IQV3_GEOTN            Unreviewed;       512 AA.
AC   A4IQV3;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 105.
DE   RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 2 {ECO:0000256|HAMAP-Rule:MF_00713};
DE            EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine cleavage system P-protein subunit 2 {ECO:0000256|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine decarboxylase subunit 2 {ECO:0000256|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 2 {ECO:0000256|HAMAP-Rule:MF_00713};
GN   Name=gcvPB {ECO:0000256|HAMAP-Rule:MF_00713};
GN   OrderedLocusNames=GTNG_2362 {ECO:0000313|EMBL:ABO67707.1};
OS   Geobacillus thermodenitrificans (strain NG80-2).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=420246 {ECO:0000313|EMBL:ABO67707.1, ECO:0000313|Proteomes:UP000001578};
RN   [1] {ECO:0000313|EMBL:ABO67707.1, ECO:0000313|Proteomes:UP000001578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NG80-2 {ECO:0000313|EMBL:ABO67707.1,
RC   ECO:0000313|Proteomes:UP000001578};
RX   PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA   Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA   Han W., Peng X., Liu R., Wang L.;
RT   "Genome and proteome of long-chain alkane degrading Geobacillus
RT   thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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:0000256|ARBA:ARBA00003788, ECO:0000256|HAMAP-
CC       Rule:MF_00713}.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00033655, ECO:0000256|HAMAP-
CC         Rule:MF_00713};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|HAMAP-Rule:MF_00713};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. In this organism, the P 'protein' is a heterodimer of two
CC       subunits. {ECO:0000256|HAMAP-Rule:MF_00713}.
CC   -!- SIMILARITY: Belongs to the GcvP family. C-terminal subunit subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00713}.
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DR   EMBL; CP000557; ABO67707.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4IQV3; -.
DR   KEGG; gtn:GTNG_2362; -.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_5_0_9; -.
DR   OMA; MHINLHK; -.
DR   Proteomes; UP000001578; 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; 1.
DR   Gene3D; 6.20.440.10; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   HAMAP; MF_00713; GcvPB; 1.
DR   InterPro; IPR023012; GcvPB.
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   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; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00713}; Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00713}.
FT   DOMAIN          33..303
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          352..455
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
FT   MOD_RES         272
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00713"
SQ   SEQUENCE   512 AA;  56369 MW;  9017F25D6C1040BB CRC64;
     MHNDQPLIFE RSKPGRIAYS LPTLDVPAVD VSELVPADYL RTEEPELPEV SELDLMRHYT
     ALSKRNHGVD SGFYPLGSCT MKYNPKINEN VARLAGFAHI HPLQPEETVQ GALELMYDLQ
     EHLKEITGMD AVTLQPAAGA HGEWTGLMMI RAYHEANGDF GRTKVIVPDS AHGTNPASAT
     VAGFETVTVR STADGLVDLE DLKRVVGPDT AALMLTNPNT LGLFEEQIVE MAEIVHEAGG
     KLYYDGANLN AILGKARPGD MGFDVVHLNL HKTFTGPHGG GGPGSGPVGV KADLIPFLPK
     PVIAKGENGY YLDDDRPQSI GRVKPFYGNF GINVRAYTYI RSMGPDGLKA VSEYAVLNAN
     YMMRRLADYY DLPYNRHCKH EFVLSGKRQK KLGVRTLDIA KRLLDFGFHP PTIYFPLIVE
     ECMMIEPTET ESKETLDAFI DAMIQIAKEA EETPEIVQEA PHTTVVKRLD ETTAARKRDF
     ALSKNEKLIP ISGSSKNGRA VSFSPAAPLL QR
//
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