ID A0A257M778_9BACT Unreviewed; 944 AA.
AC A0A257M778;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:OYV07452.1};
GN ORFNames=CFE26_00960 {ECO:0000313|EMBL:OYV07452.1};
OS Verrucomicrobiales bacterium VVV1.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales.
OX NCBI_TaxID=2015575 {ECO:0000313|EMBL:OYV07452.1, ECO:0000313|Proteomes:UP000216473};
RN [1] {ECO:0000313|EMBL:OYV07452.1, ECO:0000313|Proteomes:UP000216473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VVV1 {ECO:0000313|EMBL:OYV07452.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
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:OYV07452.1}.
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DR EMBL; NKJB01000015; OYV07452.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257M778; -.
DR Proteomes; UP000216473; 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:UP000216473}.
FT DOMAIN 10..434
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 463..721
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 761..882
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 693
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 944 AA; 101505 MW; 2864446A3547DEF5 CRC64;
MSARIDFLSR HLGPVDTERD EMLRTVGFDS LDALVDAAVP AGIRLDQPMD LPPARSEQEA
LGWLKSIFSK NVVMKSFIGQ GYHGTFVPPV VQRNILENPG WYTAYTPYQA EIAQGRLEAL
LNFQTMITDL TGLDVSNASL LDEGTAAAEA MSLALSSKPK GRAIFVSDRC HPQTIDVVVT
RAEPLGIEVI VGDWATFDPG ATANLFAVLV QYPDTRGRID DFTTFFEKAH AAGAVTIAAA
DLLALTVLKA PGSFGADICI GSSQRFGVPM GFGGPHAAVM ACRDDLKRKM PGRLIGISID
SRGKPGYRLS LQTREQHIRR DKATSNICTA QVLLAVMASM YAVYHGPEGL KHIAHTVHAR
TAQLKSLLAT AGIETESGPF FDTLVAIVPG KASEVHERAL RAGVNLRNLG PDRVGISFDE
TTSEGDVLLV ISAFGGAGEL PDIASVAWSA ELSRDTPYLT QAAFNRFHSE TEMLRYMKRL
ESKDLALNDS MIALGSCTMK LNATAEMMPL SWPEVSSIHP FVPADQSTGY REMLTLLEDW
LATVTGFAAV SLQPNAGSQG EYAGLLAIRR YHLARGDSHR NVCLIPVSAH GTNPASAVMT
GMKVVGVKCD DKGNIDVGDL EARIAEHREN LSCLMVTYPS THGVFEETIV DICEKIHAAG
GQVYMDGANM NAQVGLTSPG FIGADVCHLN LHKTFCIPHG GGGPGVGPIG VAKQLVPYLP
GHRELSEHEG SVCSAPWGSA SINTISWMYI AMMGADGLKA ATATAILTAN YAAKRLSPFY
PILYTGNMGL VAHECIIDVR PLSDKSGITV EDVAKRLMDY GFHAPTMSWP VGGTLMIEPT
ESESKVEIDR FCDSMIAIHG EIMAVINGEA DAHDNPLKNA PHPAEVICAD EWTHAYSREQ
AAYPLPGLRQ HKFWPSVGRI DNVHGDRNLV CTCDSVEAYA AAGA
//
