ID A0A255HLY0_9BURK Unreviewed; 968 AA.
AC A0A255HLY0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:OYO29240.1};
GN ORFNames=CD932_19310 {ECO:0000313|EMBL:OYO29240.1};
OS Janthinobacterium sp. PC23-8.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=2012679 {ECO:0000313|EMBL:OYO29240.1, ECO:0000313|Proteomes:UP000216749};
RN [1] {ECO:0000313|EMBL:OYO29240.1, ECO:0000313|Proteomes:UP000216749}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC23-8 {ECO:0000313|EMBL:OYO29240.1,
RC ECO:0000313|Proteomes:UP000216749};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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:OYO29240.1}.
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DR EMBL; NJGY01000002; OYO29240.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255HLY0; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000216749; 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 18..443
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 457..749
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 787..908
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 712
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 968 AA; 104051 MW; 73BFCE79ED8E108F CRC64;
MTRTSLTQLE ARDAFIARHI GPSPSEQEAM LSTLGYASRA ALIDALVPAN IRNQGALPLG
AYSQPMPEQE ALSRLKAIAG KNQVLKSMIG QGYYNTFTPG VVLRNIFENP AWYTAYTPYQ
PEISQGRLEA ILNFQQVITD LTGMGIANAS MLDEGTAAAE AMTLIQRVGK SKSTVLYVAS
DVLPQTLEVV QTRALPIGIE VRMFDPAEID ALGECFGVLL QYPGVNGVVR DYRAGVEKLH
AGGAMVIVAA DLLALTMLTP PGEWGADVVV GNSQRFGVPL GFGGPHAGYL STRDAFKRNM
SGRLVGVTVD AQGNKAYRLA LQTREQHIRR EKATSNICTA QVLLAVMASM YAVYHGPVGL
LQIARRVHRF TGVLAANLTT LGHKVVNQTY FDTLTIQVAD ADQLHATAIA HGVNLRKIDG
QHVGLSLDET TTRDDIALLW TIFAQGVANA PAAPDLDSVE AAVENALPAH LVRTSAYLTH
PVFNSYHSEH EMLRYLRSLA DKDLALDRTM IPLGSCTMKL NATSEMIPVT WPEFSNIHPF
APDAQTVGYR EMIAQLEDML CALTGYAAVS LQPNAGSQGE YAGLLVIKAY HESRGEGHRN
ICLIPSSAHG TNPASANMVG MQVVVTSCDA NGNVDLADLK AKAEKHSANL ACVMVTYPST
HGVFEEGIQE LCEIIHSHGG QVYIDGANMN ALVGVAAPGS FGGDVSHLNL HKTFCIPHGG
GGPGVGPIGV GAHLAKFLPN QRSSGYQRDA YDAGIGAVSS APFGSASILP ISWMYIAMMG
AEGLTAATET AILAANYIAR RLSPHYPVLY TGHDGLVAHE CILDLRPITD ATGISNEDVA
KRLMDFGFHA PTMSFPVPGT LMIEPTESES KVEMDRFIDA MIAIRHEIAK VASGEFDHDD
NPLKNAPHTA QVLLADDWNR KYSRSVAAYP VASLRERKYW PPVGRADNVY GDRNLFCGCA
PISSYEEA
//
