ID U2Z4N6_9RHOB Unreviewed; 622 AA.
AC U2Z4N6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Epi-inositol hydrolase {ECO:0000313|EMBL:GAD56340.1};
GN ORFNames=MBELCI_2392 {ECO:0000313|EMBL:GAD56340.1};
OS Limimaricola cinnabarinus LL-001.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Limimaricola.
OX NCBI_TaxID=1337093 {ECO:0000313|EMBL:GAD56340.1, ECO:0000313|Proteomes:UP000016566};
RN [1] {ECO:0000313|EMBL:GAD56340.1, ECO:0000313|Proteomes:UP000016566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL-001 {ECO:0000313|EMBL:GAD56340.1,
RC ECO:0000313|Proteomes:UP000016566};
RA Nishi S., Tsubouchi T., Takaki Y., Koyanagi R., Satoh N., Maruyama T.,
RA Hatada Y.;
RT "Draft Genome Sequence of Loktanella cinnabarina LL-001T, Isolated from
RT Deep-Sea Floor Sediment.";
RL Genome Announc. 1:e00927-13(2013).
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:GAD56340.1}.
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DR EMBL; BATB01000034; GAD56340.1; -; Genomic_DNA.
DR AlphaFoldDB; U2Z4N6; -.
DR STRING; 1337093.MBELCI_2392; -.
DR eggNOG; COG3962; Bacteria.
DR Proteomes; UP000016566; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; IPR000399; TPP-bd_CS.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:GAD56340.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..136
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 223..356
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 439..573
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 622 AA; 66874 MW; 50D434A78F3A4213 CRC64;
MTASQGTVRL TTAQAIIRWL ANQYIEIDGE ELRVCGGGFG IFGHGNVTCL GEALHGVQEA
LPLYRGQNEQ GMGFAAAGYA KQWLRQRFMF CTASAGPGTM NLLTAAGLAH ANRLPMLLLC
GDGFLTRLPT PVLQQMENYG DPTFGVNDAF KPVVRYWDRI THPAQVIQSL PAALATLLDP
ADCGPAFIGL PQDVQGWAWD FPDAMFEKKV HRIRRIAPDE AEIADARAAL LAAKRPMIIA
GGGVQYARAA EDLAAFAEAH RIPVVETIAG RANLLAEHPL NIGPIGVTGS DSANAIAAEA
DLILAVGTRL QDFTTGSWTA FDAEARIVAI NAARHDAGKH RALPVVGDAK RALDALGQGL
DYAAPAAWVD KAQKERRDWD AYVAGNVKPG NGPNSYAQAI GVVNELCHPR DRIVAAAGGL
PAEVTANWRT LGIGTVDVEF GFSCMGYEIS GAWGARIAQE QREPEPDTIV FIGDGSYMMM
NSDLYSAALS RKKLIVLVLD NGGFAVINKL QNNTGNESFN NLLADCPTIP EPFAVDFEAH
ARSQGAEAVT VENSAELGAA FERAKASTRS QVIVMKVDPY DAWTTRGHAW WEVGTPEVTT
NDRVRAAHED QEQGRARQRR GV
//
