ID C6DYX2_GEOSM Unreviewed; 479 AA.
AC C6DYX2;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN OrderedLocusNames=GM21_0392 {ECO:0000313|EMBL:ACT16473.1};
OS Geobacter sp. (strain M21).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=443144 {ECO:0000313|EMBL:ACT16473.1};
RN [1] {ECO:0000313|EMBL:ACT16473.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M21 {ECO:0000313|EMBL:ACT16473.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Lovley D.;
RT "Complete sequence of Geobacter sp. M21.";
RL Submitted (JUL-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};
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DR EMBL; CP001661; ACT16473.1; -; Genomic_DNA.
DR AlphaFoldDB; C6DYX2; -.
DR STRING; 443144.GM21_0392; -.
DR KEGG; gem:GM21_0392; -.
DR eggNOG; COG1003; Bacteria.
DR HOGENOM; CLU_004620_5_0_7; -.
DR OrthoDB; 9801272at2; -.
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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR049316; GDC-P_C.
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; PF00266; Aminotran_5; 1.
DR Pfam; PF21478; GcvP2_C; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ACT16473.1}.
FT DOMAIN 145..273
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 348..442
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
SQ SEQUENCE 479 AA; 51990 MW; BBA12C822F65390B CRC64;
MQLIFEKSVP GRSGVRVPLS DVPKASPFPA ALRRKEPVLL PEVSELDLVR HYTNLSRRNF
SVDTNFYPLG SCTMKYNTKV TEDAGGLFAG CHPVLPLLPG GERLVQGPLS LIHGLEQQLV
EITGMDEVTT QPLAGAHGEM TGIMVIAAYH KARNDQKRKY VIVPDSSHGT NPASAAMAGY
EIVTIPTAPY GDMDLEQFKN AMNDEVAAVM MTCPNTLGLF NPHIAEICAI AHAAGALTYY
DGANLNAILG KVRPGDVGFD VIHVNLHKTF GTPHGGGGPG SGPVGVKKAL IPYLPTPRVQ
RKGDGSFAVA AHPEGIGRVS DFFGNFAIMA RAYAYITLLG CEGLIEVSEH AVLNANYMMA
RLKGEYELPF EQTCMHECVF SASRQLKDGV HAIDIAKYLI DRGFHPPTVY FPLNVKEAIM
IEPTETESKQ TMDLFIDVML EAARLAREDP EALHRAPVTT PVGRLDETRA ARAQQVCCE
//
