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Database: UniProt
Entry: D1VXR2_9BACT
LinkDB: D1VXR2_9BACT
Original site: D1VXR2_9BACT 
ID   D1VXR2_9BACT            Unreviewed;       480 AA.
AC   D1VXR2;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE            EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN   ORFNames=HMPREF9019_1896 {ECO:0000313|EMBL:EFA97985.1};
OS   Hoylesella timonensis CRIS 5C-B1.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Hoylesella.
OX   NCBI_TaxID=679189 {ECO:0000313|EMBL:EFA97985.1, ECO:0000313|Proteomes:UP000004001};
RN   [1] {ECO:0000313|EMBL:EFA97985.1, ECO:0000313|Proteomes:UP000004001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRIS 5C-B1 {ECO:0000313|EMBL:EFA97985.1,
RC   ECO:0000313|Proteomes:UP000004001};
RA   Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Strausberg R.L.,
RA   Nelson K.E.;
RT   "Genome Sequence of Prevotella timonensis CRIS 5C-B1.";
RL   Submitted (DEC-2009) 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   -!- 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:EFA97985.1}.
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DR   EMBL; ADEF01000015; EFA97985.1; -; Genomic_DNA.
DR   RefSeq; WP_008122772.1; NZ_ADEF01000015.1.
DR   AlphaFoldDB; D1VXR2; -.
DR   eggNOG; COG1003; Bacteria.
DR   Proteomes; UP000004001; Unassembled WGS sequence.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR   Gene3D; 6.20.440.10; -; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
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   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; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EFA97985.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004001}.
FT   DOMAIN          27..297
FT                   /note="Glycine cleavage system P-protein N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02347"
FT   DOMAIN          344..442
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
SQ   SEQUENCE   480 AA;  53056 MW;  F8D123FD5149400E CRC64;
     MNHQLYHNLI FELSHPGRRG YTLPKNEFGR HEIPATLKRT VDAELPECDE LTVVRHYTNH
     SENNFGVDNG FYPLGSCTMK YNPTINEEIA AHPAFVNLHP LQPAETVQGA KEVYENLQQA
     LSALTGLSRF TLNPCAGAHG ELTGLMIISA YHQANNDTKR TKIIVPDSAH GTNPASAAVC
     GLEVVEVKST ADGLVDVEHL KTLLGDDIAG MMMTNPNTLG LFETHIPEIT KLIHDCGGLM
     YYDGANLNPL LGECRPGDMG FDVMHINLHK TFSTPHGGGG PGSGPVGVCE KLVDFLPTNN
     CATNAKGHFT ITVHPYHGHF LTYLRAYTYI LTLGKENIKM VGPYATLNAN YIKECLKDVY
     KLPIDTICKH EFVFDGLMDK STGVTTMDVA KRLLDHGFHA PTIYFPLLFH EAMMIEPTEN
     ESKETLDAFI EVMRKIADEA KNDPEIVKSA PQETPIKRVN DVEAAKHPIL TFKQLIDDNN
//
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