ID A3V3Y6_9RHOB Unreviewed; 613 AA.
AC A3V3Y6;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Iold protein {ECO:0000313|EMBL:EAQ07193.1};
GN ORFNames=SKA53_02316 {ECO:0000313|EMBL:EAQ07193.1};
OS Yoonia vestfoldensis SKA53.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Yoonia.
OX NCBI_TaxID=314232 {ECO:0000313|EMBL:EAQ07193.1, ECO:0000313|Proteomes:UP000004507};
RN [1] {ECO:0000313|EMBL:EAQ07193.1, ECO:0000313|Proteomes:UP000004507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA53 {ECO:0000313|EMBL:EAQ07193.1,
RC ECO:0000313|Proteomes:UP000004507};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (JAN-2006) 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:EAQ07193.1}.
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DR EMBL; AAMS01000003; EAQ07193.1; -; Genomic_DNA.
DR AlphaFoldDB; A3V3Y6; -.
DR STRING; 314232.SKA53_02316; -.
DR eggNOG; COG3962; Bacteria.
DR HOGENOM; CLU_013748_6_0_5; -.
DR Proteomes; UP000004507; 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 Reference proteome {ECO:0000313|Proteomes:UP000004507};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 36..132
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 222..354
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 415..568
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 613 AA; 65452 MW; E35FA56547F447F3 CRC64;
MTPMTKTIRL TAAQAMVRYV AAQMNGNGEQ FIAGCWAIFG HGNVAGIGEA LYHVKENLPT
YRGHNEQTMA HAAIAYAKQL GRKRAMMVTS SIGPGATNMV TAAALAHVNR LPVLLVPGDV
FANRGPDPVL QQIEDFNDGT ISVNDVFKPV SRYFDRITRP EQLLTALPRA FRTMTDPADC
GPVTLAFCQD VQAEAYDYPE SFFAPKVWTT RRIRPDLEEL VALAEAIKDA QCPVIVAGGG
VHYSGATDAL RAFADAHNIP VTETQAGKSA LAWDHPLNLG PIGVTGGTPA NTVCAKADLV
LGVGTRFQDF TTGSWGLFAN PARRIACLNV AAYDAAKHDA LPLLADAKVG LEALSEALGE
HFAKTPVTGL KSDWFDKVDP LTDAPSDTHA LPTDMQVVGA VQRAATDATV VMCAAGTMPG
ELHKLWKSAR PMSYHMEYGF SCMGYEIAGA MGIKMAQPDR DVICFTGDGT YMMANAELAT
AAMMGIAFTV VVTDNRGYGC INRLQMATGG AEFNNLLDHS VHAQPSAIDF AAHAASMGAT
SVKVSSIAEL EVALASRSDM QGPYVVVIDT DPYPSTPHGG TWWDVGVPQV SQRAKVIAAR
ADYESNKTKQ RAD
//
