ID W5Y2W7_9CORY Unreviewed; 939 AA.
AC W5Y2W7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN ORFNames=B843_09175 {ECO:0000313|EMBL:AHI23220.1};
OS Corynebacterium vitaeruminis DSM 20294.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1224164 {ECO:0000313|EMBL:AHI23220.1, ECO:0000313|Proteomes:UP000019222};
RN [1] {ECO:0000313|EMBL:AHI23220.1, ECO:0000313|Proteomes:UP000019222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10234 {ECO:0000313|Proteomes:UP000019222};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "The complete genome sequence of Corynebacterium vitaeruminis DSM 20294.";
RL Submitted (FEB-2013) 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}.
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};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC 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}.
CC -!- SIMILARITY: Belongs to the GcvP family.
CC {ECO:0000256|ARBA:ARBA00010756}.
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DR EMBL; CP004353; AHI23220.1; -; Genomic_DNA.
DR RefSeq; WP_051483487.1; NZ_CP004353.1.
DR AlphaFoldDB; W5Y2W7; -.
DR STRING; 1224164.B843_09175; -.
DR KEGG; cvt:B843_09175; -.
DR PATRIC; fig|1224164.3.peg.1852; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_2_1_11; -.
DR Proteomes; UP000019222; Chromosome.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR CDD; cd00613; GDC-P; 1.
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 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,
KW ECO:0000313|EMBL:AHI23220.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR603437-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000019222}.
FT DOMAIN 5..427
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 448..713
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 756..877
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 686
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 939 AA; 100139 MW; B4530C8C83CBDDFF CRC64;
MTFARRHVGP DSHEQQLMLE AVGYASIDDL LDAAIPSGIR TTDDLGLGPG LSEAQAAERL
RAYAKQNTVL KAFYGQGFYD TITPPVIRRN VVEDPGWYTA YTPYQPEISQ GRLEALLNFQ
TMVEELTGLP VANASLLDEA SAVAEAVGLM GRVHRKGNRV VLDEALHPQV LAVATARART
IGIEVEVADL AQGLVGEGVI GIVAAYPGTE GEVTDIRQAI NDVHSRGGLA AVACDLLALQ
LLESPGALGA DIAVGSSQRF GVPLFYGGPH AAFMAVTDAI KRQMPGRIVG VSVDADERPA
YRLALQTREQ HIRREKATSN ICTAQALLAV CASMYAVWHG PEGLKAIAER VHGLACAFAE
ALEDGGVDLA HQRFFDTVTV VVPGRAEEIV AGLAAKGYLV RAIGADKVSV AFGESANEAD
VRMLADAFGV VVDKHDAAPR LPKALARTTP TLTHPVFSSI HSETQMLRYL RGLKDKDLAL
DRTMIPLGSC TMKLNPTTGM EPITWPEFAN MHPYAPKEQA AGWLGLIADL EGWLAEITGY
AKVSLQPNAG SQGELAGLNA IRRYHLSRGD DQRDIILIPQ SAHGTNAASA TLANLRVAVV
ATAADGSIDL GDLDEKLAKH EHHVAGIMIT YPSTHGVFEE SVRKVCAKVH AAGGQVYIDG
ANLNALAGYA RPGEFGGDVS HLNLHKTFTI PHGGGGPGVG PVAVAEHLVP FLPTDPTLPQ
RGPGVPVAST FYGSAGVLPI SWAYIAMMGD EGLRQATANA ILNANYVAAS LRESFPVLYT
GESGLVAHEC IFDLRSLTDA TGATATDVAK RLVDYGFHAP TLSFPVAGTL MVEPTESEDK
GELDRFIAAM RSIRAEIEEV ARGDYAYEDS VLHHAPFTAE SVIADSWTHP FSREKAAYPL
RSLRGGDKYF PPVRRLNEAY GDRNFACSCP PPSAFDFGN
//
