ELTD_MYCS2
ID ELTD_MYCS2 Reviewed; 362 AA.
AC A0QXD8;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Erythritol/L-threitol dehydrogenase {ECO:0000303|PubMed:26560079};
DE EC=1.1.1.- {ECO:0000269|PubMed:26560079};
GN Name=eltD {ECO:0000303|PubMed:26560079};
GN OrderedLocusNames=MSMEG_3265 {ECO:0000312|EMBL:ABK76018.1},
GN MSMEI_3181 {ECO:0000312|EMBL:AFP39644.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, INDUCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=26560079; DOI=10.1021/jacs.5b08968;
RA Huang H., Carter M.S., Vetting M.W., Al-Obaidi N., Patskovsky Y.,
RA Almo S.C., Gerlt J.A.;
RT "A general strategy for the discovery of metabolic pathways: D-threitol, L-
RT threitol, and erythritol utilization in Mycobacterium smegmatis.";
RL J. Am. Chem. Soc. 137:14570-14573(2015).
CC -!- FUNCTION: Catalyzes the NAD-dependent reversible oxidation of
CC erythritol and L-threitol. Involved in the degradation pathways of
CC erythritol and L-threitol, that allow M.smegmatis to grow on these
CC compounds as the sole carbon source. {ECO:0000269|PubMed:26560079}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=erythritol + NAD(+) = D-erythrulose + H(+) + NADH;
CC Xref=Rhea:RHEA:48756, ChEBI:CHEBI:15378, ChEBI:CHEBI:16023,
CC ChEBI:CHEBI:17113, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:26560079};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threitol + NAD(+) = H(+) + L-erythrulose + NADH;
CC Xref=Rhea:RHEA:48760, ChEBI:CHEBI:15378, ChEBI:CHEBI:27913,
CC ChEBI:CHEBI:42090, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:26560079};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O58389};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:O58389};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.64 mM for L-threitol {ECO:0000269|PubMed:26560079};
CC KM=1.50 mM for erythritol {ECO:0000269|PubMed:26560079};
CC KM=1.47 mM for L-arabitol {ECO:0000269|PubMed:26560079};
CC KM=2.76 mM for xylitol {ECO:0000269|PubMed:26560079};
CC KM=2.21 mM for ribitol {ECO:0000269|PubMed:26560079};
CC KM=0.026 mM for D-erythrulose {ECO:0000269|PubMed:26560079};
CC KM=0.066 mM for L-erythrulose {ECO:0000269|PubMed:26560079};
CC KM=0.73 mM for D-xylulose {ECO:0000269|PubMed:26560079};
CC KM=0.25 mM for L-xylulose {ECO:0000269|PubMed:26560079};
CC KM=1.23 mM for ribulose {ECO:0000269|PubMed:26560079};
CC Note=kcat is 10.2 sec(-1) with L-threitol as substrate. kcat is 8.46
CC sec(-1) with erythritol as substrate. kcat is 8.73 sec(-1) with L-
CC arabitol as substrate. kcat is 8.20 sec(-1) with xylitol as
CC substrate. kcat is 6.56 sec(-1) with ribitol as substrate. kcat is
CC 9.88 sec(-1) with D-erythrulose as substrate. kcat is 13.3 sec(-1)
CC with L-erythrulose as substrate. kcat is 19.3 sec(-1) with D-xylulose
CC as substrate. kcat is 7.75 sec(-1) with L-xylulose as substrate. kcat
CC is 21.0 sec(-1) with ribulose as substrate.
CC {ECO:0000269|PubMed:26560079};
CC -!- PATHWAY: Carbohydrate metabolism; erythritol degradation.
CC {ECO:0000269|PubMed:26560079}.
CC -!- PATHWAY: Carbohydrate metabolism; L-threitol degradation.
CC {ECO:0000269|PubMed:26560079}.
CC -!- INDUCTION: Up-regulated during growth on erythritol, D-threitol or L-
CC threitol relative to growth on glycerol. {ECO:0000269|PubMed:26560079}.
CC -!- DISRUPTION PHENOTYPE: Complete loss of the ability to grow on
CC erythritol or on L-threitol. {ECO:0000269|PubMed:26560079}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; CP000480; ABK76018.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39644.1; -; Genomic_DNA.
DR RefSeq; WP_011728938.1; NZ_SIJM01000015.1.
DR RefSeq; YP_887576.1; NC_008596.1.
DR AlphaFoldDB; A0QXD8; -.
DR SMR; A0QXD8; -.
DR STRING; 246196.MSMEI_3181; -.
DR PRIDE; A0QXD8; -.
DR EnsemblBacteria; ABK76018; ABK76018; MSMEG_3265.
DR EnsemblBacteria; AFP39644; AFP39644; MSMEI_3181.
DR GeneID; 66734665; -.
DR KEGG; msg:MSMEI_3181; -.
DR KEGG; msm:MSMEG_3265; -.
DR PATRIC; fig|246196.19.peg.3226; -.
DR eggNOG; COG1063; Bacteria.
DR OMA; DDICTHQ; -.
DR OrthoDB; 972769at2; -.
DR BioCyc; MetaCyc:MON-19889; -.
DR UniPathway; UPA01066; -.
DR UniPathway; UPA01067; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0016052; P:carbohydrate catabolic process; IMP:UniProtKB.
DR GO; GO:0009758; P:carbohydrate utilization; IMP:UniProtKB.
DR GO; GO:0071322; P:cellular response to carbohydrate stimulus; IDA:UniProtKB.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Metal-binding; NAD; Oxidoreductase;
KW Reference proteome; Zinc.
FT CHAIN 1..362
FT /note="Erythritol/L-threitol dehydrogenase"
FT /id="PRO_0000435513"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 195
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 215
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O58389"
SQ SEQUENCE 362 AA; 39356 MW; 2A52D2595D723E0E CRC64;
MSNQVPEKMQ AVVCHGPHDY RLEEVAVPQR KPGEALIRVE AVGICASDLK CYHGAAKFWG
DENRPAWAET MVIPGHEFVG RVVELDDEAA QRWGIAVGDR VVSEQIVPCW ECLFCKRGQY
HMCQPHDLYG FKRRTPGAMA SYMVYPAEAL VHKVSPDIPA QHAAFAEPLS CSLHAVERAQ
ITFEDTVVVA GCGPIGLGMI AGAKAKSPMR VIALDMAPDK LKLAEKCGAD LTINIAEQDA
EKIIKDLTGG YGADVYIEGT GHTSAVPQGL NLLRKLGRYV EYGVFGSDVT VDWSIISDDK
ELDVLGAHLG PYCWPAAIKM IESGALPMDE ICTHQFPLTE FQKGLDLVAS GKESVKVSLI
PA
