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Database: UniProt
Entry: A0A0D8HHN9_9ACTN
LinkDB: A0A0D8HHN9_9ACTN
Original site: A0A0D8HHN9_9ACTN 
ID   A0A0D8HHN9_9ACTN        Unreviewed;       595 AA.
AC   A0A0D8HHN9;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Acetolactate synthase isozyme 3 large subunit {ECO:0000313|EMBL:KJF17428.1};
DE            EC=2.2.1.6 {ECO:0000313|EMBL:KJF17428.1};
GN   Name=ilvI {ECO:0000313|EMBL:KJF17428.1};
GN   ORFNames=AXFE_17060 {ECO:0000313|EMBL:KJF17428.1};
OS   Acidithrix ferrooxidans.
OC   Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC   Acidimicrobiaceae; Acidithrix.
OX   NCBI_TaxID=1280514 {ECO:0000313|EMBL:KJF17428.1, ECO:0000313|Proteomes:UP000032360};
RN   [1] {ECO:0000313|EMBL:KJF17428.1, ECO:0000313|Proteomes:UP000032360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Py-F3 {ECO:0000313|EMBL:KJF17428.1,
RC   ECO:0000313|Proteomes:UP000032360};
RA   Poehlein A., Eisen S., Schloemann M., Johnson B.D., Daniel R., Muehling M.;
RT   "Draft genome of the acidophilic iron oxidizer Acidithrix ferrooxidans
RT   strain Py-F3.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KJF17428.1}.
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DR   EMBL; JXYS01000042; KJF17428.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D8HHN9; -.
DR   STRING; 1280514.AXFE_17060; -.
DR   PATRIC; fig|1280514.3.peg.2237; -.
DR   Proteomes; UP000032360; Unassembled WGS sequence.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd00568; TPP_enzymes; 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; 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   PANTHER; PTHR18968:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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:UP000032360};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000313|EMBL:KJF17428.1}.
FT   DOMAIN          18..131
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          215..349
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          417..570
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   595 AA;  64357 MW;  1C1705094CDE2C33 CRC64;
     MTVESEKVAS IDVTNPSMTG AEALVKQLEL YGVEYVFGLC GHTNIAVLDA LSRSPIEFII
     NRHEQTAAHA ADGYARASGK PGVLLSHVGP GMINAATGVY TAALDSVPLI AIAGDVPSYY
     YGRHPHQEIN IHNNASQADV YRPFVKRAWN VERVEDLVRF TERAFWTATS GRPGAVLLNV
     PMDMFSRRLP STYNFPPPLP ARSTSPRLGY GVAESIATML VDANRPLIYL GGGIRTKEGL
     AALVSLAEHL DIPIAHSLMG KGAVSDDHPL VIGMTGFWGS TFTNGYAREA DVVLGLATRF
     AETDSSSWMP EYTWQFPPSR LIQIDIDPDE IGRNYPVEIG AVADVNQAVI EIEAALKIMA
     KDGVNKPELR EDIKAMREGL WARTKENGSS DQFPLRPERI LQDLLETLPS DAVLVTDVGW
     NKNGVAQGYK LPSQGKFITP GGASTMGFGP AGAIGVQIAL PDRTVIALIG DGGMSAQLPA
     VPTAVEQGLP IIWVVMNNRA HGTIADLEYG NYGHSFGTIF QDRNGASYSP DFAAYARACG
     ADGYAISSPQ EFKKSLLDAL ELRRPALLDV PMVNEPVPTP GHWNINDIYQ GRFFD
//
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