IOLM_THEMA
ID IOLM_THEMA Reviewed; 395 AA.
AC Q9WYP3; G4FHX1;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=scyllo-inosose 3-dehydrogenase {ECO:0000305|PubMed:23441918};
DE EC=1.1.1.- {ECO:0000269|PubMed:23441918};
DE AltName: Full=2-keto-myo-inositol dehydrogenase {ECO:0000303|PubMed:23441918};
GN Name=iolM {ECO:0000303|PubMed:23441918};
GN OrderedLocusNames=TM_0412 {ECO:0000312|EMBL:AAD35497.1};
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, PATHWAY, AND SUBUNIT.
RX PubMed=23441918; DOI=10.1111/1462-2920.12096;
RA Rodionova I.A., Leyn S.A., Burkart M.D., Boucher N., Noll K.M.,
RA Osterman A.L., Rodionov D.A.;
RT "Novel inositol catabolic pathway in Thermotoga maritima.";
RL Environ. Microbiol. 15:2254-2266(2013).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) IN COMPLEX WITH CADMIUM IONS, AND
RP COFACTOR.
RA Ramagopal U.A., Toro R., Burley S.K., Almo S.C.;
RT "Structure of putative alcohol dehydrogenase (TM_042) from Thermotoga
RT maritima.";
RL Submitted (AUG-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of scyllo-inosose
CC (2-keto-myo-inositol) to 3-dehydro-scyllo-inosose (diketo-inositol),
CC and thus probably functions in a myo-inositol degradation pathway
CC together with IolG, IolN and IolO. Has no activity on myo-inositol, D-
CC chiro-inositol and 1-keto-D-chiro-inositol.
CC {ECO:0000269|PubMed:23441918}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + scyllo-inosose = 3-dehydro-scyllo-inosose + H(+) +
CC NADH; Xref=Rhea:RHEA:53284, ChEBI:CHEBI:15378, ChEBI:CHEBI:17811,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:137015;
CC Evidence={ECO:0000269|PubMed:23441918};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|Ref.3};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000305|Ref.3};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.7 mM for scyllo-inosose {ECO:0000269|PubMed:23441918};
CC KM=0.14 mM for NAD(+) {ECO:0000269|PubMed:23441918};
CC Note=kcat is 1 sec(-1). {ECO:0000269|PubMed:23441918};
CC -!- PATHWAY: Polyol metabolism; myo-inositol metabolism.
CC {ECO:0000305|PubMed:23441918}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23441918}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AE000512; AAD35497.1; -; Genomic_DNA.
DR PIR; B72381; B72381.
DR RefSeq; NP_228222.1; NC_000853.1.
DR RefSeq; WP_004083260.1; NZ_CP011107.1.
DR PDB; 3IP1; X-ray; 2.09 A; A/B/C/D=2-395.
DR PDBsum; 3IP1; -.
DR AlphaFoldDB; Q9WYP3; -.
DR SMR; Q9WYP3; -.
DR STRING; 243274.THEMA_02665; -.
DR DNASU; 897413; -.
DR EnsemblBacteria; AAD35497; AAD35497; TM_0412.
DR KEGG; tma:TM0412; -.
DR PATRIC; fig|243274.17.peg.410; -.
DR eggNOG; COG1063; Bacteria.
DR InParanoid; Q9WYP3; -.
DR OMA; CCRNFGT; -.
DR OrthoDB; 972769at2; -.
DR BioCyc; MetaCyc:MON-17949; -.
DR UniPathway; UPA00914; -.
DR EvolutionaryTrace; Q9WYP3; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006020; P:inositol metabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
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.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..395
FT /note="scyllo-inosose 3-dehydrogenase"
FT /id="PRO_0000440855"
FT ACT_SITE 68
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT ACT_SITE 71
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:3IP1"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:3IP1"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:3IP1"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:3IP1"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:3IP1"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:3IP1"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:3IP1"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000305|Ref.3, ECO:0007744|PDB:3IP1"
FT BINDING 223
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT BINDING 248
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O58389"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:3IP1"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:3IP1"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 35..45
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:3IP1"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:3IP1"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3IP1"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:3IP1"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3IP1"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 158..166
FT /evidence="ECO:0007829|PDB:3IP1"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:3IP1"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:3IP1"
FT HELIX 183..190
FT /evidence="ECO:0007829|PDB:3IP1"
FT HELIX 192..202
FT /evidence="ECO:0007829|PDB:3IP1"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:3IP1"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 237..242
FT /evidence="ECO:0007829|PDB:3IP1"
FT HELIX 246..255
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:3IP1"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:3IP1"
FT HELIX 268..275
FT /evidence="ECO:0007829|PDB:3IP1"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:3IP1"
FT HELIX 291..304
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:3IP1"
FT HELIX 326..331
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:3IP1"
FT HELIX 347..356
FT /evidence="ECO:0007829|PDB:3IP1"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:3IP1"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:3IP1"
FT HELIX 374..380
FT /evidence="ECO:0007829|PDB:3IP1"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:3IP1"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:3IP1"
SQ SEQUENCE 395 AA; 43317 MW; 29D2A19F00946397 CRC64;
MRAVRLHAKW DPRPEFKLGP KDIEGKLTWL GSKVWRYPEV RVEEVPEPRI EKPTEIIIKV
KACGICGSDV HMAQTDEEGY ILYPGLTGFP VTLGHEFSGV VVEAGPEAIN RRTNKRFEIG
EPVCAEEMLW CGHCRPCAEG FPNHCENLNE LGFNVDGAFA EYVKVDAKYA WSLRELEGVY
EGDRLFLAGS LVEPTSVAYN AVIVRGGGIR PGDNVVILGG GPIGLAAVAI LKHAGASKVI
LSEPSEVRRN LAKELGADHV IDPTKENFVE AVLDYTNGLG AKLFLEATGV PQLVWPQIEE
VIWRARGINA TVAIVARADA KIPLTGEVFQ VRRAQIVGSQ GHSGHGTFPR VISLMASGMD
MTKIISKTVS MEEIPEYIKR LQTDKSLVKV TMLNE
