ID A0A0T9QE55_9GAMM Unreviewed; 959 AA.
AC A0A0T9QE55;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
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 ECO:0000313|EMBL:CNI07606.1};
GN ORFNames=ERS008529_02997 {ECO:0000313|EMBL:CNI07606.1};
OS Yersinia pekkanenii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=1288385 {ECO:0000313|EMBL:CNI07606.1, ECO:0000313|Proteomes:UP000045840};
RN [1] {ECO:0000313|Proteomes:UP000045840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A125KOH2 {ECO:0000313|Proteomes:UP000045840};
RG Pathogen Informatics;
RL Submitted (MAR-2015) 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}.
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DR EMBL; CQAZ01000027; CNI07606.1; -; Genomic_DNA.
DR RefSeq; WP_049613948.1; NZ_CWJL01000024.1.
DR AlphaFoldDB; A0A0T9QE55; -.
DR STRING; 1288385.ERS137968_03823; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000045840; 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}.
FT DOMAIN 16..440
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 477..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; 104843 MW; 9C8ACDE0DC1E64DD CRC64;
MTQNLSQLEH NDAFIQRHIG SSTEQQQQML AAIGASSLST LIQQIVPADI QLPSPPPVGD
AATEHQALAE LKGIASQNQC YKSYIGMGYS PVLTPPVILR NMLENPGWYT AYTPYQPEVS
QGRLEALLNF QQLTQDLTGL DLASASLLDE ATAAAESMAL AKRASKLKDT NRFFVADDVH
PQTLDVVRTR AETFGFEVIV DRAEKVLELE GVFGVLLQQV GTTGELHDYS VLLVELKSRK
IITSVAADIM TLVLLTAPGK QGADVVFGSA QRFGVPMGYG GPHAAFFACR DEFKRSMPGR
IIGVSRDAAG NTALRMAMQT REQHIRREKA NSNICTSQVL LANIASLYAV YHGPQGLQRI
AGRIHRMTDI LAVGLQQAGL TLRFQHWFDT LTVEVKDKAA VLARALSFGI NLRTDIHGAV
GITLDETTSR DDLQTLFALL AGDNHGLDID QLDARVSQNS QSIQNTMLRQ DPILTHPVFN
RYHSETEMMR YMHRLERKDL ALNQAMIPLG SCTMKLNAAA EMIPITWPEF AELHPFCPPE
QAAGYQQMIS QLSQWLVQLT GYDAVCMQPN SGAQGEYAGL LAIRRYHESG NQANRHICLI
PSSAHGTNPA SAQMAGMSVV VVACDKQGNI DLHDLRQKAG EAGDELSCIM VTYPSTHGVY
EETIREVCQI VHQFGGQVYL DGANMNAQVG ITTPGYIGAD VSHLNLHKTF CIPHGGGGPG
MGPIGVKAHL APFVPGHSVV QIDGMTTQQG AVSAAPFGSA SILPISWMYI RMMGADGLKQ
ASQVAILNAN YIATRLKEAY PVLYIGHDGR VAHECILDIR PLKEATGISE MDIAKRLIDF
GFHAPTMSFP VAGTLMVEPT ESESKTELDR FIDAMLAIRA EIEKVARGEW PLEDNPLVNA
PHTQAELVGN WQHPYSRELA VFPVAGVMEN KYWPAVKRLD DVYGDRNLFC SCVPVSDYE
//
