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
//