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Database: UniProt
Entry: A0A0M2WG45_9BURK
LinkDB: A0A0M2WG45_9BURK
Original site: A0A0M2WG45_9BURK 
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
//
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