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Database: UniProt
Entry: A0A0W0YVE1_9GAMM
LinkDB: A0A0W0YVE1_9GAMM
Original site: A0A0W0YVE1_9GAMM 
ID   A0A0W0YVE1_9GAMM        Unreviewed;       622 AA.
AC   A0A0W0YVE1;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Myo-inositol catabolism protein IolD {ECO:0000313|EMBL:KTD60486.1};
GN   Name=iolD {ECO:0000313|EMBL:KTD60486.1};
GN   ORFNames=Lsha_1582 {ECO:0000313|EMBL:KTD60486.1};
OS   Legionella shakespearei DSM 23087.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=1122169 {ECO:0000313|EMBL:KTD60486.1, ECO:0000313|Proteomes:UP000054600};
RN   [1] {ECO:0000313|EMBL:KTD60486.1, ECO:0000313|Proteomes:UP000054600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49655 {ECO:0000313|EMBL:KTD60486.1,
RC   ECO:0000313|Proteomes:UP000054600};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:KTD60486.1}.
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DR   EMBL; LNYW01000044; KTD60486.1; -; Genomic_DNA.
DR   RefSeq; WP_018578171.1; NZ_LNYW01000044.1.
DR   AlphaFoldDB; A0A0W0YVE1; -.
DR   STRING; 1122169.Lsha_1582; -.
DR   PATRIC; fig|1122169.6.peg.1822; -.
DR   eggNOG; COG3962; Bacteria.
DR   OrthoDB; 3194735at2; -.
DR   Proteomes; UP000054600; Unassembled WGS sequence.
DR   GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR   GO; GO:0019310; P:inositol catabolic process; IEA:InterPro.
DR   CDD; cd02003; TPP_IolD; 1.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR030817; Myo_inos_IolD.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   NCBIfam; TIGR04377; myo_inos_iolD; 1.
DR   PANTHER; PTHR18968:SF9; 3D-(3,5/4)-TRIHYDROXYCYCLOHEXANE-1,2-DIONE HYDROLASE; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054600};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          7..130
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          218..351
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          416..577
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   622 AA;  68075 MW;  253C5CB68D478420 CRC64;
     MKIKLTMAQA LLKFLANQYV AIDGQEQQFV HGVFGIFGHG NVTGLGEALE YDSNGLIFYQ
     GHNEQGMAHA ATAYAKQKNR LGILACTSSI GPGATNMITA AATATTNRIP LLLLPGDIFS
     SRQPDPVLQQ LEVPHDYSIS VNDCFKPVSK YWDRISRPEQ LVTACMQAMR VLTDPAETGA
     VTLCLPQDVQ AESFEYDSSF FAKRVWHIER DALSERAVAA AVHLLRHAQK PLIIAGGGVH
     YSFATECLAD FATRHAIPVA ETQAGKSSLS AEHPLNAGGI GVTGSEVANC LAAQADVLLV
     VGSRLQDFTT ASKWGFKNPE CQIIHLNVSR LDAMKMNALM LKGDAKTGLE QISLKLGTYQ
     TPVSYQHLIQ QYQREWSLER AKVCSPPKES TGLHQTAVLE MINQFAKPDD VVIGAAGSLP
     GDLHRLWKSK KPKDYHLEYA YSCMGYEVAA GLGVRLAKGN SPGEVYVLVG DGSFVMMHSE
     LLTSIQEHKK ITVVIFDNHG FQCIRNLQEG NGSQGFGNEF RYRHAQTNRL TGNYLPVDFC
     LYAAGLGAKT FLAESYEQLG SALEQAQAQE QTSVIVVPVL PKTMSHGYQT WWRVGVAEVS
     KSDAVLAAHE AMEEQVKYTK MY
//
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