ID L0FWL9_ECHVK Unreviewed; 966 AA.
AC L0FWL9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 OrderedLocusNames=Echvi_0744 {ECO:0000313|EMBL:AGA77020.1};
OS Echinicola vietnamensis (strain DSM 17526 / LMG 23754 / KMM 6221).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Echinicola.
OX NCBI_TaxID=926556 {ECO:0000313|EMBL:AGA77020.1, ECO:0000313|Proteomes:UP000010796};
RN [1] {ECO:0000313|Proteomes:UP000010796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17526 / LMG 23754 / KMM 6221
RC {ECO:0000313|Proteomes:UP000010796};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Echinicola vietnamensis DSM 17526.";
RL Submitted (FEB-2012) 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}.
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DR EMBL; CP003346; AGA77020.1; -; Genomic_DNA.
DR RefSeq; WP_015264586.1; NC_019904.1.
DR AlphaFoldDB; L0FWL9; -.
DR STRING; 926556.Echvi_0744; -.
DR KEGG; evi:Echvi_0744; -.
DR PATRIC; fig|926556.3.peg.746; -.
DR eggNOG; COG0403; Bacteria.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_3_2_10; -.
DR OrthoDB; 9801272at2; -.
DR Proteomes; UP000010796; Chromosome.
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:UP000010796}.
FT DOMAIN 13..441
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 481..737
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
FT DOMAIN 782..902
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT MOD_RES 710
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00711,
FT ECO:0000256|PIRSR:PIRSR603437-50"
SQ SEQUENCE 966 AA; 106459 MW; B20E77BA7E9C5EDE CRC64;
MKIDLTPSVK FEDRHNGPSA NDVSEMLSKI GASSIDELID QTIPKAIQLD QPLNLPEAKS
EAAFLKDFRK MAAKNKIYKS FIGLGYYDTI TPGVILRNVL ENPGWYTAYT PYQAEIAQGR
LEALVNFQTM VMDLTGMELA NASLLDEGTA AAEAMNMLFA TRPRDKKKAT KFFVDEKVFI
QTKEILKTRA LPIGVTLVEG SLNELNLEDP ELYGVLLQYP NAEGEAIDYK ALVEKAKQHN
VTTAFSADLL ALTLLTPPGE MGADVVVGTT QRFGVPMGFG GPHAAYFATK DAYKRQVPGR
IIGISVDKDG NKAYRMALQT REQHIKRERA TSNICTAQVL LAVMAGMYAV YHGPKGLKDI
ALKIHGLAKL TAQGLAKLGF EQENEHYFDT LKIKVDDVKQ SKIKAFALSH EMNFRYEPGY
VYLAFDEAKT MEDVQEIIEV FARTTHSSAD VVDLASMVDH LSFEVSDGLR RTSDYMDHMI
FNAFHSEHEM LRYIKRLENR DLSLVHSMIS LGSCTMKLNA TAEMIPVTWP EFGQLHPFVP
QDQAAGYYAL FQDLRNWLSE ITGFAETSLQ PNSGAQGEFA GLMVIRAYHE SRGESHRNIA
LIPSSAHGTN PASAVMAGMK VVIVKCDDKG NIDLADLKEK AEKHKENLSS FLVTYPSTHG
VFEEAIREMC QIVHENGGQV YMDGANMNAQ VGLTSPGVIG ADVCHLNLHK TFCIPHGGGG
PGMGPICVAK HLEEFLPSSP LVKTGGQQPI SAISAAPFGS ASILPISYAY IAMMGREGLK
HATQTAILNA NYIKARLGEF FPTLYTGAQG RAAHEMIVDF REFKAVGVEV EDIAKRLIDY
GFHSPTVSFP VAGTMMIEPT ESESKAELDR FCDALIAIRG EIREIEEGKA DAENNVLKNA
PHTAGMVMSD AWDMPYSREK AVYPLEYVKN SKFWPTVRRI DSAYGDRNLV CSCIPTEDYA
EEAAGI
//
