ID A0A0T2KXY8_9MICO Unreviewed; 316 AA.
AC A0A0T2KXY8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glucose dehydrogenase {ECO:0000313|EMBL:KRA24527.1};
GN ORFNames=ASD65_08925 {ECO:0000313|EMBL:KRA24527.1};
OS Microbacterium sp. Root61.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736570 {ECO:0000313|EMBL:KRA24527.1, ECO:0000313|Proteomes:UP000051216};
RN [1] {ECO:0000313|EMBL:KRA24527.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA24527.1,
RC ECO:0000313|Proteomes:UP000051216};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA24527.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA24527.1,
RC ECO:0000313|Proteomes:UP000051216};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DapA family.
CC {ECO:0000256|PIRNR:PIRNR001365}.
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:KRA24527.1}.
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DR EMBL; LMGU01000001; KRA24527.1; -; Genomic_DNA.
DR RefSeq; WP_056221378.1; NZ_LMGU01000001.1.
DR AlphaFoldDB; A0A0T2KXY8; -.
DR STRING; 1736570.ASD65_08925; -.
DR OrthoDB; 3175637at2; -.
DR Proteomes; UP000051216; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR CDD; cd00408; DHDPS-like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002220; DapA-like.
DR InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR PANTHER; PTHR12128:SF72; 4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12128; DIHYDRODIPICOLINATE SYNTHASE; 1.
DR Pfam; PF00701; DHDPS; 1.
DR PIRSF; PIRSF001365; DHDPS; 1.
DR PRINTS; PR00146; DHPICSNTHASE.
DR SMART; SM01130; DHDPS; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00666; DHDPS_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW Reference proteome {ECO:0000313|Proteomes:UP000051216};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT ACT_SITE 142
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT ACT_SITE 170
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT BINDING 215
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ SEQUENCE 316 AA; 32722 MW; C44E44C44C04E5D6 CRC64;
MTITTSSTAQ LSGVVPPVVT PLLPDGSIDV ASLEHLVEYL ISSGVSGLFA LGSSGETAYF
TDDQRVEILT VIARANAGRL PIIAGAIELT SARVIETARR LIAAGADTIV TTAPLYAINS
PSETAAHFRA VAAGIDAPLW AYDVPVRVHS KLSADLLVQL GTEGVIEGVK DSSGDDVGFR
RLIAANAAAG SPLRLFTGHE VVVDAMALAG ADGVVPGLAN VEAAGYVRLW DAAGQGDWDT
ARAEQERLNR LFEIVFQTSG LSPDAAGVGA FKTAMVARGI IAQATMAFPV QPLPGEAVER
IWAILESMDL LAAPVA
//
