DTHD_MYCS2
ID DTHD_MYCS2 Reviewed; 260 AA.
AC A0QYC2;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=D-threitol dehydrogenase {ECO:0000303|PubMed:26560079};
DE EC=1.1.1.403 {ECO:0000269|PubMed:26560079};
GN Name=dthD {ECO:0000303|PubMed:26560079};
GN OrderedLocusNames=MSMEG_3607 {ECO:0000312|EMBL:ABK74381.1},
GN MSMEI_3523 {ECO:0000312|EMBL:AFP39986.1};
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 D-
CC threitol. Involved in the degradation pathway of D-threitol, that
CC allows M.smegmatis to grow on this compound as the sole carbon source.
CC Does not catalyze the oxidation of xylitol, L-sorbitol, and L-sorbose.
CC {ECO:0000269|PubMed:26560079}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threitol + NAD(+) = D-erythrulose + H(+) + NADH;
CC Xref=Rhea:RHEA:48748, ChEBI:CHEBI:15378, ChEBI:CHEBI:16023,
CC ChEBI:CHEBI:48300, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.403; Evidence={ECO:0000269|PubMed:26560079};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.52 mM for D-threitol {ECO:0000269|PubMed:26560079};
CC KM=1.20 mM for D-threose {ECO:0000269|PubMed:26560079};
CC KM=0.048 mM for D-erythrulose {ECO:0000269|PubMed:26560079};
CC Note=kcat is 6.97 sec(-1) with D-threitol as substrate. kcat is 0.71
CC sec(-1) with D-threose as substrate. kcat is 7.32 sec(-1) with D-
CC erythrulose as substrate. {ECO:0000269|PubMed:26560079};
CC -!- PATHWAY: Carbohydrate metabolism; D-threitol degradation.
CC {ECO:0000269|PubMed:26560079}.
CC -!- INDUCTION: Up-regulated during growth on D-threitol relative to growth
CC on glycerol. {ECO:0000269|PubMed:26560079}.
CC -!- DISRUPTION PHENOTYPE: Complete loss of the ability to grow on D-
CC threitol. {ECO:0000269|PubMed:26560079}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; CP000480; ABK74381.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP39986.1; -; Genomic_DNA.
DR RefSeq; WP_011729199.1; NZ_SIJM01000008.1.
DR RefSeq; YP_887910.1; NC_008596.1.
DR AlphaFoldDB; A0QYC2; -.
DR SMR; A0QYC2; -.
DR STRING; 246196.MSMEI_3523; -.
DR EnsemblBacteria; ABK74381; ABK74381; MSMEG_3607.
DR EnsemblBacteria; AFP39986; AFP39986; MSMEI_3523.
DR GeneID; 66734992; -.
DR KEGG; msg:MSMEI_3523; -.
DR KEGG; msm:MSMEG_3607; -.
DR PATRIC; fig|246196.19.peg.3556; -.
DR eggNOG; COG1028; Bacteria.
DR OMA; HKICHFR; -.
DR OrthoDB; 1294334at2; -.
DR BioCyc; MetaCyc:MON-19892; -.
DR BRENDA; 1.1.1.403; 3512.
DR UniPathway; UPA01065; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0047880; F:erythrulose reductase activity; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..260
FT /note="D-threitol dehydrogenase"
FT /id="PRO_0000435514"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 21..50
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4W1"
FT BINDING 170
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4W1"
SQ SEQUENCE 260 AA; 26333 MW; A7E529EA57C7D3AF CRC64;
MTQAQELSVD FDFRLDGKVA LVTGAASGIG AAIASAYATK GARIAAVDLN AEGAEALAAQ
LGGDRGAHRG FACDVADAAS VQAAADAVAA EFGRIDILVN SAGVARLAPA EELSLQDWDS
TLAINLSGTF LMCQAVGKRM LEAGGGAIVN MASQAATVAL DQHVAYCASK FGVVGVSKVL
AAEWGGRGVR VNTISPTVVL TELGHKAWDG PRGDALKKLI PTGRFAYPDE IAAAAVFLAS
DAAAMINGAD LVIDGGYTIK
