ID A0A0M2WG45_9BURK Unreviewed; 966 AA.
AC A0A0M2WG45;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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:KKO61836.1};
GN ORFNames=VM94_03907 {ECO:0000313|EMBL:KKO61836.1};
OS Janthinobacterium sp. KBS0711.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=1649647 {ECO:0000313|EMBL:KKO61836.1, ECO:0000313|Proteomes:UP000034315};
RN [1] {ECO:0000313|EMBL:KKO61836.1, ECO:0000313|Proteomes:UP000034315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS0711 {ECO:0000313|EMBL:KKO61836.1,
RC ECO:0000313|Proteomes:UP000034315};
RA Shoemaker W.R., Muscarella M.E., Lennon J.T.;
RT "Genome sequence of the soil bacterium Jantinobacterium sp. KBS0711.";
RL Submitted (APR-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}.
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:KKO61836.1}.
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DR EMBL; LBCO01000033; KKO61836.1; -; Genomic_DNA.
DR RefSeq; WP_046685527.1; NZ_VCCE02000001.1.
DR AlphaFoldDB; A0A0M2WG45; -.
DR PATRIC; fig|1649647.5.peg.4007; -.
DR Proteomes; UP000034315; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000034315}.
FT DOMAIN 18..443
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 458..754
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 785..906
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 966 AA; 103852 MW; 69DE69E5A030C079 CRC64;
MTRTSLTQLE ARDAFIARHI GPSATEQQAM LATLGYPSRA ALIDALVPAN IRNKGALPLG
AYSQPMPEQE ALSRLKAIAG KNQVLKSLIG QGYYNTFTPG VVLRNIFENP AWYTAYTPYQ
PEISQGRLEA ILNFQQVITD LTGMGISNAS MLDEGTAAAE AMTLIQRVGK SKSNVLYVAN
DVLPQTLEVV QTRAQPIGIE VRTFDPAEIE SLDACFGVLL QYPGVNGVVR DYRAGVEKLH
ANGAMVIVAA DLLALTMLTP PGEWGADVVV GNSQRFGVPL GFGGPHAGYL STRDEFKRNM
SGRLVGVTVD AQGNKAYRLA LQTREQHIRR EKATSNICTA QVLLAVMASM YAVYHGPAGL
LQIAQRVHRF TGVLAANLKT LGYGVVNASY FDTLTINVAD AAQLHATAMH HGVNLRKIDN
THVGVSLDET TTRDDIALLW KVFAHGLANA PAAPDLDAVE ATVTSALPAN LARESAYLTH
PVFNSYHSEH EMLRYLRSLA DKDLALDRTM IPLGSCTMKL NATSEMIPVT WPEFSNIHPF
APDAQTVGYR EMIAQLEEML CALTGYAAVS LQPNAGSQGE YAGLLVIKAY HESRGEGHRN
ICLIPSSAHG TNPASANMVG MQVVVTSCDA NGNVDLADLK AKAEKHSANL ACVMVTYPST
HGVFEEGIQE LCEIIHAHGG QVYIDGANMN ALVGVAAPGS FGGDVSHLNL HKTFCIPHGG
GGPGVGPIGV GTHLAKFLPN QRSSGYQRDA AGIGAVSAAP FGSASILPIS WMYIAMMGAE
GLTAATETAI LAANYIARRL APHYPVLYSG HDGLVAHECI LDLRPITDAT GISNEDVAKR
LMDFGFHAPT MSFPVPGTLM IEPTESESKV EIDRFIDAMI AIRAEIAKVA SGEFDHDDNP
LRNAPHTAQV LMSDSWDRKY SREIAAYPVA SLRQRKYWPP VGRADNVYGD RNLFCGCAPI
SSYEEE
//