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Database: UniProt
Entry: A1WKP6_VEREI
LinkDB: A1WKP6_VEREI
Original site: A1WKP6_VEREI 
ID   A1WKP6_VEREI            Unreviewed;       531 AA.
AC   A1WKP6;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE            EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN   OrderedLocusNames=Veis_2458 {ECO:0000313|EMBL:ABM58203.1};
OS   Verminephrobacter eiseniae (strain EF01-2).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Verminephrobacter.
OX   NCBI_TaxID=391735 {ECO:0000313|EMBL:ABM58203.1, ECO:0000313|Proteomes:UP000000374};
RN   [1] {ECO:0000313|Proteomes:UP000000374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF01-2 {ECO:0000313|Proteomes:UP000000374};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL   Submitted (DEC-2006) 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; CP000542; ABM58203.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1WKP6; -.
DR   STRING; 391735.Veis_2458; -.
DR   KEGG; vei:Veis_2458; -.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_5_0_4; -.
DR   Proteomes; UP000000374; Chromosome.
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:ABM58203.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000374}.
FT   DOMAIN          185..304
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   DOMAIN          381..488
FT                   /note="Glycine dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21478"
SQ   SEQUENCE   531 AA;  58816 MW;  ECF0964D1B68A2AE CRC64;
     MRKEPMQDIS AARFTRGQPH LRRYHQARWD EPVIFELSQP GERALLLPEV EPAIAATAAA
     PLPPGMRRAQ APALPQLSQN RVLRHYLRLS QETLGADLNV DIGQGTCTMK YNPKINEQLA
     RDERISQLHP LQDESTVQGM LQVMHEMEHV IEEVSGMDAV SLQPRSGSQA IYANIAMVRA
     WFEARGEAGQ RDEIITTIFS HPSDAACAKV VGYKVITLYP DADGYPDLAA MQAAVGPRTA
     ALVITNPEDT GIFNPRIAQF VQAAHDVGAL ACYDQANANG LLGITRARDA GFDLCHFNLH
     KTFATPHACG GPAVGACAVT QALAPFLPHP RIVKDGQRYR LQTDEKTSIG KVAAFMGAAS
     IVLRAYAWVM NLGADGLREV AEVAVLNNNY VMRQLLQIKG LSAPYANGKS RIEQVRYSWR
     ELSEETGVHA EDIGLRAADY GVHYWTSHHP YIVAEPATIE PTEAYSRADL DEFVQIMAHI
     ADEARSTPQT VTSAPHRCPT RRVDTKYLED PRQWAMTWRA WRRKLAEHGA R
//
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