ID A0A0N1N4T6_9PROT Unreviewed; 623 AA.
AC A0A0N1N4T6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase {ECO:0000313|EMBL:KPH86748.1};
GN ORFNames=GLUCOINTEAF2_0200666 {ECO:0000313|EMBL:KPH86748.1};
OS Komagataeibacter intermedius AF2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Komagataeibacter.
OX NCBI_TaxID=1458464 {ECO:0000313|EMBL:KPH86748.1, ECO:0000313|Proteomes:UP000031553};
RN [1] {ECO:0000313|EMBL:KPH86748.1, ECO:0000313|Proteomes:UP000031553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF2 {ECO:0000313|EMBL:KPH86748.1,
RC ECO:0000313|Proteomes:UP000031553};
RA Santos R.A., Berretta A.A., Barud H.S., Ribeiro S.J., Gonzalez-Garcia L.N.,
RA Zucchi T.D., Goldman G.H., Riano-Pachon D.M.;
RT "Draft Genome Sequence of Komagataeibacter intermedius Strain AF2, Isolated
RT from Kombucha Tea.";
RL Submitted (JUL-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:KPH86748.1}.
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DR EMBL; JUFX02000192; KPH86748.1; -; Genomic_DNA.
DR RefSeq; WP_039735791.1; NZ_JUFX02000192.1.
DR AlphaFoldDB; A0A0N1N4T6; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000031553; 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:0019310; P:inositol catabolic process; IEA:InterPro.
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 Hydrolase {ECO:0000313|EMBL:KPH86748.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 9..133
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 222..353
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 422..576
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 623 AA; 67255 MW; CB1DC2E6F1ECFC89 CRC64;
MTQATIRLTT AQAIVQWLVN QFTEIEGQRV PLFPGVFGIF GHGNVSCLSE ALEAVQDRLP
TWRGQNEQSM ALAATGFAKA RRRRQIMVAT SSIGPGALNM VTAAGTAHAN RLPLLLLAGD
TFATRLPDPV LQQVEHFSNP TITVNDAFRA VTRYWDRIMH PAQILSSLPQ ATATMLDPGD
CGPAFVSLPQ DVQEIAFDYP VTFFEEKLWA IPRPRPDRRR LAQAVDLLKT ARKPLLIAGG
GVRYSQAEEA VAAFALKRGI PIVETIAGKG SVTHYHEAHA GPIGIIGSTS ANALAGDADV
IVAIGTRLQD FTTGSWTLFS QTARFISINT ARFDAVKHRA LAVVGDALET ITEFDTLLGD
WTADPRQMQR ARLLFGEWDD LLTKLQAPTN APVPTYAQVV HAVNDAAGEC DTIITAAGGL
PGEVCKGWRV KAPNTFDLEF GFSCMGYEIA AGWGHAMASE GPGGTGGTPI VMIGDGTYMM
MNSDIYSTVL TGHKMIVVVC DNGGFAVINR LQQAKGVPGF NNLLVDCHVQ HPDRPLHVDF
VKHAESMGAL GRRCDSMAEL ATALEWAKTT DRTTILAITT DAHAWTPGDA DWDVGVPEVS
TRASVQTARK QQEEIRAKQR VGV
//
