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Database: UniProt
Entry: Q2SMT8_HAHCH
LinkDB: Q2SMT8_HAHCH
Original site: Q2SMT8_HAHCH 
ID   Q2SMT8_HAHCH            Unreviewed;       616 AA.
AC   Q2SMT8;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:ABC28036.1};
GN   Name=iolD {ECO:0000313|EMBL:ABC28036.1};
GN   OrderedLocusNames=HCH_01159 {ECO:0000313|EMBL:ABC28036.1};
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC28036.1, ECO:0000313|Proteomes:UP000000238};
RN   [1] {ECO:0000313|EMBL:ABC28036.1, ECO:0000313|Proteomes:UP000000238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC28036.1,
RC   ECO:0000313|Proteomes:UP000000238};
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP000155; ABC28036.1; -; Genomic_DNA.
DR   RefSeq; WP_011395111.1; NC_007645.1.
DR   AlphaFoldDB; Q2SMT8; -.
DR   STRING; 349521.HCH_01159; -.
DR   KEGG; hch:HCH_01159; -.
DR   eggNOG; COG3962; Bacteria.
DR   HOGENOM; CLU_013748_6_0_6; -.
DR   OrthoDB; 3194735at2; -.
DR   Proteomes; UP000000238; Chromosome.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000000238};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          7..131
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          220..352
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          418..569
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   616 AA;  66454 MW;  4A69CCA6DC3795F9 CRC64;
     MKTIRLTMAQ AVIKYMIAQK VDVDGEIKPL FAGMWAIFGH GNVAGLGEAL HHVRDALPTY
     RAHNEQGMAH AAIAYAKTQN RRQMMACTAS AGPGSVNMVT AAAVAHVNRI PVLFLPGDTF
     ATRIPDPVLQ QVENFHDYTL TSNDCFKPVS RFFDRITRPE QLLASLPQAL RVLTDPVECG
     PVTLALPQDV QTMAFDYPES FFVEKIHRLR RQAPDATELA DAIAMIKASK KPLLVAGGGV
     HYSGALAELD RLASTYALPV GETQAGKGAL PWDHRQNIGS LGVTGAASTN ALAAEADLII
     AVGTRLGDFA SGSRAIIDPH AKLLSINVAS FDAIKHKGQP LVGDARLTLA QLQDALGDWR
     PDGEWIEKAE RLRAQWHKTV DNATADHQAD LPTDAEVVGA VNRAAGEKDI VVCAAGGLPG
     DLQKLWRTRY DRGYHLEYGY SCMGYELAGG VGAKMAKPDS DVFVMVGDGS YLMLNSEIAT
     SVMLGQKIII VVLDNRGFGC IHRLQQACGG PGFNNLLDDC LTADGGAPKI DFAAHGAALG
     AKSESVRNIK ELEAALERAK ASDISYLIAI DTDPLKVTED GGAWWDVAVA EVSERPQVEE
     ARRRYESFKA RQFKNL
//
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