ID A0A095TDH5_9GAMM Unreviewed; 959 AA.
AC A0A095TDH5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000256|HAMAP-Rule:MF_00711};
DE EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine cleavage system P-protein {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine decarboxylase {ECO:0000256|HAMAP-Rule:MF_00711};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|HAMAP-Rule:MF_00711};
GN Name=gcvP {ECO:0000256|HAMAP-Rule:MF_00711};
GN ORFNames=HA49_06665 {ECO:0000313|EMBL:KGD74961.1};
OS Tatumella morbirosei.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Tatumella.
OX NCBI_TaxID=642227 {ECO:0000313|EMBL:KGD74961.1, ECO:0000313|Proteomes:UP000029577};
RN [1] {ECO:0000313|EMBL:KGD74961.1, ECO:0000313|Proteomes:UP000029577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 23360 {ECO:0000313|EMBL:KGD74961.1,
RC ECO:0000313|Proteomes:UP000029577};
RA Smits T.H., Palmer M., Venter S.N., Duffy B., Steenkamp E.T., Chan W.Y.,
RA Coutinho T.A., Coetzee M.P., De Maayer P.;
RT "The draft genome of the Tatumella morbirosei type strain, LMG23360T
RT isolated from pineapple rot.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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_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;
CC Evidence={ECO:0000256|ARBA:ARBA00043839, ECO:0000256|HAMAP-
CC Rule:MF_00711};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00711, 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, ECO:0000256|HAMAP-
CC Rule:MF_00711}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000256|ARBA:ARBA00010756,
CC ECO:0000256|HAMAP-Rule:MF_00711}.
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:KGD74961.1}.
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DR EMBL; JPKR02000004; KGD74961.1; -; Genomic_DNA.
DR RefSeq; WP_038018132.1; NZ_JPKR02000004.1.
DR AlphaFoldDB; A0A095TDH5; -.
DR STRING; 642227.HA49_06665; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000029577; Unassembled WGS sequence.
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:SF13; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 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, ECO:0000256|HAMAP-
KW Rule:MF_00711};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00711}; Reference proteome {ECO:0000313|Proteomes:UP000029577}.
FT DOMAIN 17..440
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 450..739
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 781..902
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 708
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 959 AA; 105049 MW; E39ECDF437DFF0FC CRC64;
MTRTLSQLEN QNDFISRHIG PTEQQQQTML QSIGADSLPA LINAIVPQSI RLPELPATGE
AVTEQQALAE LKAIAGKNKC YKSWIGMGYS AVITPPVILR NLLENPGWYT AYTPYQPEVS
QGRLEALLNF QQLTLDLTGM DIASASLLDE ATAAAEAMAM AKRVSKLKNA NKFFVADDVH
PQTLDVVRTR AETFGFELII DAAERAADHQ DLFGVLLQYC GTRGHLHDYR EIIAQLKQRK
VIVSVAADFM ALVLLTSPGA QGADIVFGSS QRFGVPMGYG GPHAAFFASR DEHKRAMPGR
IIGVSRDVSG NQALRMAMQT REQHIRREKA NSNICTSQVL LANIAGMYAV WHGPQGLKTI
AERIHRMTDI LAAALQQRGM KIRNLQWFDT LMVEVKDKAA VLQRAAEHQV NLRTDLHQAV
GITLDETTVR QDLQTLITIL TGDTAPADIE SLDQLLAAES HSIPQALYRT DAILSHPVFN
RYHSETEMMR YLHRLEKKDL ALNQAMIPLG SCTMKLNAAA EMLPITWPEF AGLHPFCPTS
QAAGYLQMID MLSRWLVQLT GYDALCMQPN SGAQGEYAGL LAIRRYHESR QQPERNICLI
PASAHGTNPA SAQMAGMEVV VVACDKQGNI DLDDLRLKAG QAGEQLSCIM VTYPSTHGVY
EATIGEVCEI VHQHGGQVYL DGANMNAQVG LTSPGFIGAD VSHLNLHKTF CIPHGGGGPG
MGPIGVKAHL APFVPGHSVV QLDGVLTREG AVSAAPFGSA SILPISWMYI RMMGAEGLRQ
ASSVAILNAN YIARRLSDAY PILYTGAHGH VAHECILDIR PLKEQTGISE MDIAKRLIDY
GFHAPTMSFP VAGTLMVEPT ESESQQELDR FIAAMLAIRS EIDKVAAGEW PADDNPLVNA
PHTQQEITGD WQHSYSREQA VFPAGSEDKY WPTVKRLDDV YGDRNLFCSC VPISDYQAQ
//
