ID T1BTE6_9ZZZZ Unreviewed; 491 AA.
AC T1BTE6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=glycine dehydrogenase (aminomethyl-transferring) {ECO:0000256|ARBA:ARBA00012134};
DE EC=1.4.4.2 {ECO:0000256|ARBA:ARBA00012134};
GN ORFNames=B1B_04236 {ECO:0000313|EMBL:EQD71823.1};
OS mine drainage metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=410659 {ECO:0000313|EMBL:EQD71823.1};
RN [1] {ECO:0000313|EMBL:EQD71823.1}
RP NUCLEOTIDE SEQUENCE.
RA Mendez C., Richter M., Ferrer M., Sanchez J.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EQD71823.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24430486; DOI=10.1038/ismej.2013.242;
RA Mendez-Garcia C., Mesa V., Sprenger R.R., Richter M., Diez M.S., Solano J.,
RA Bargiela R., Golyshina O.V., Manteca A., Ramos J.L., Gallego J.R.,
RA Llorente I., Martins Dos Santos V.A., Jensen O.N., Pelaez A.I., Sanchez J.,
RA Ferrer M.;
RT "Microbial stratification in low pH oxic and suboxic macroscopic growths
RT along an acid mine drainage.";
RL ISME J. 8:1259-1274(2014).
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 -!- 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:EQD71823.1}.
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DR EMBL; AUZY01002658; EQD71823.1; -; Genomic_DNA.
DR AlphaFoldDB; T1BTE6; -.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; 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 HAMAP; MF_00713; GcvPB; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR023012; GcvPB.
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 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 154..273
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 349..451
FT /note="Glycine dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21478"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 491 AA; 54360 MW; 0C1D0A2EA0597D7A CRC64;
MSALIFDHSR PGRRAPGLAP EQEESIDDLP QALLRRHPPP LPEVSELEVV RHYTRLSQKN
FSIDTHFYPL GSCTMKYNPR AANRLAMLAG FLDTHPLAPA RTRQGFLACV FELQEMLQTA
TGMSAVVLSP MAGAQGEFAG MDMIRRYHRA RNDEARNEVL VPDAAHGTNP ASAVMAGFRV
REIPTDREGD VDMAALRAAV GPKTAGIMLT NPSTLGVFER RILDIAKIVH QAGGLLYYDG
ANLNAILGRV RPGDMQFDVL HLNLHKTFST PHGGGGPGAA ALGVGPTLEP YLPVPFVAKD
ATGGLSWVEE ESRPETIGRL SAFMGNGGVL LRAYVYARLL GRTGMRRVSE YATLNANYLA
RRLEEAGFEL AYPRRRTSHE CIVTLRREAR EMGVTAMDFA KRLLDYGMHA PTTYFPLLVP
ECLLIEPTET ESLETLDAFV DAMIRIREEA RSDPDRVRHA PWTTPVRRLD DVRAARELDL
AWRSDSDPDR T
//
