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Database: UniProt
Entry: F0GGT0_9BURK
LinkDB: F0GGT0_9BURK
Original site: F0GGT0_9BURK 
ID   F0GGT0_9BURK            Unreviewed;       614 AA.
AC   F0GGT0;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE            EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
DE   Flags: Fragment;
GN   ORFNames=B1M_37291 {ECO:0000313|EMBL:EGC99302.1};
OS   Burkholderia sp. TJI49.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=987057 {ECO:0000313|EMBL:EGC99302.1, ECO:0000313|Proteomes:UP000003049};
RN   [1] {ECO:0000313|EMBL:EGC99302.1, ECO:0000313|Proteomes:UP000003049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TJI49 {ECO:0000313|EMBL:EGC99302.1,
RC   ECO:0000313|Proteomes:UP000003049};
RX   PubMed=23653265; DOI=10.1007/s11274-013-1366-5;
RA   Khan A., Asif H., Studholme D.J., Khan I.A., Azim M.K.;
RT   "Genome characterization of a novel Burkholderia cepacia complex genomovar
RT   isolated from dieback affected mango orchards.";
RL   World J. Microbiol. Biotechnol. 29:2033-2044(2013).
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}.
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};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR603437-50};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000256|ARBA:ARBA00011690}.
CC   -!- SIMILARITY: Belongs to the GcvP family.
CC       {ECO:0000256|ARBA:ARBA00010756}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGC99302.1}.
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DR   EMBL; AEXE01002377; EGC99302.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0GGT0; -.
DR   PATRIC; fig|987057.7.peg.5741; -.
DR   Proteomes; UP000003049; Unassembled WGS sequence.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR   CDD; cd00613; GDC-P; 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   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 {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EGC99302.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50}.
FT   DOMAIN          1..93
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          133..405
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          435..556
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
FT   MOD_RES         362
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EGC99302.1"
SQ   SEQUENCE   614 AA;  65456 MW;  C74295D7656D2076 CRC64;
     AVYHGPHGLK TIALRVNRVA ALVAAGVKQL GFPIVNDTFF DTLTIDTGAR TAQVHQFAAA
     QRINLRRVSD TQVGVSVDET TTRDDLAALL AVFAQAAGGT APSVDALDAG LGGDAALPAG
     LVRTSAYLTH HVFNRHHSET EMLRYLRSLS DKDLALDRSM IPLGSCTMKL NATSEMLPVT
     WPEFGRIHPF APADQTVGYR EMIDQLEQML VAATGYAAVS LQPNAGSQGE YAGLLIIHAY
     HASRGEGHRD VCLIPASAHG TNPASAHMAG MKVVVVACDA QGNVDIADLK AKAEQHSANL
     AAIMITYPST HGVFEQNVRE ICEIVHAHGG QVYVDGANMN AMVGLTAPGQ FGGDVSHLNL
     HKTFCIPHGG GGPGVGPVAV GAHLAKFLPN QRSTGYTREE HGIGAVSAAP YGSASILPIS
     WMYIAMMGAK NLTAATETAI LNANYIAKRL APHYPVLYSG PGGLVAHECI LDLRPIKESS
     GISVDDVAKR LMDYGFHAPT MSFPVPGTLM VEPTESESQE ELDRFIAAMI AIRDEIRAVE
     EGRADREDNP LRHAPHTAAV VTANEWPHAY TREQAAYPVA SLGTNKYWPP VGRADNAYGD
     RNLFCACVPM SDYA
//
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