ID M5CPJ5_STEMA Unreviewed; 955 AA.
AC M5CPJ5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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:CCP12800.1};
GN ORFNames=SMSKK35_4270 {ECO:0000313|EMBL:CCP12800.1};
OS Stenotrophomonas maltophilia SKK35.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=1118156 {ECO:0000313|EMBL:CCP12800.1, ECO:0000313|Proteomes:UP000012178};
RN [1] {ECO:0000313|EMBL:CCP12800.1, ECO:0000313|Proteomes:UP000012178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKK35 {ECO:0000313|EMBL:CCP12800.1,
RC ECO:0000313|Proteomes:UP000012178};
RA Linke B., Adamek M., Schwartz T.;
RT "Stenotrophomonas maltophilia SKK35 and RA8 genome sequencing: analysis and
RT comparison of viurlence genes.";
RL Submitted (JUL-2012) 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:CCP12800.1}.
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DR EMBL; CALN01001101; CCP12800.1; -; Genomic_DNA.
DR AlphaFoldDB; M5CPJ5; -.
DR Proteomes; UP000012178; 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: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, ECO:0000256|HAMAP-
KW Rule:MF_00711};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00711,
KW ECO:0000256|PIRSR:PIRSR603437-50}.
FT DOMAIN 19..440
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 446..732
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 770..891
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 702
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 955 AA; 102823 MW; 343E43A360EEE040 CRC64;
MSQNTPSLRE LEHHSAFVER HIGPNDAEIA QMLDVVGHAS LDAMTDAIVP AKIKSPAPLA
LPESMTEVQA LAKIRAIADK NTVLRSFIGQ GYYGTHTPNV ILRNILENPA WYTAYTPYQA
EISQGRMEAL INFQTLCADL TGMEIANASL LDEATAAAEA MTLAKRSAKS KSDTFFVHDA
VHPQTLELLR TRAEPMGIVL RVGTPAEALE AEAFGLLLQY PDTFGQVGDY KALVDAVHAR
GGLVAVATDL LALTLLAAPG EWGADIVVGN SQRFGVPFGF GGPHAAFMAC RDAYKRSMPG
RLIGVSVDAQ GNPAYRLTLQ TREQHIRREK ATSNICTAQV LLAVMASMYA VYHGPDGLTR
IARRTHRLAS ILAAALRTAG VQVGGDFFDT LHVTGVHADE IHAKARAAGY NLRAIDSDSV
GISLDETATR ADVVALAAVF GAQADVDALD ASTADALPAG LQRQSAFLTH PVFNTHHSEH
ELLRYLRSLA DKDLAMDRTM IPLGSCTMKL NATAEMIPVT WPEFSQIHPL VPADQALGYK
ELIDTLEAML VECTGYDAVS LQPNSGAQGE YAGLLAIRAY HRSRGEGHRD ICLIPDSAHG
TNPASAQMCG MKVVVTKTDA NGNVDVEDIR LNAEKYSDRL AAIMMTYPST HGVFEEEVVE
ICEIIHQHGG QVYTDGANMN ALVGVAKPGK WGSDVSHLNL HKTFCIPHGG GGPGVGPCAV
KEHLAPFLPG KLGDHGPVGM VSAASFGSAS ILPISWMYIA MMGSEGLRKA TQVAQLNANY
IAKRLAPHFK TLYTGRNGLV AHECILDVRP LEKTSGIGAE DVAKRLIDFG FHAPTLSFPV
AGTLMVEPTE SESLHELDRF INAMIQIREE ISAIEDGRLD REDNPLKNAP HTATAVTASE
WTHAYPRELA AFPLASLKQG KYWPPVARVD NVYGDKNVMC ACIPVDAYKD DEVEA
//
