ID   A0A2U2C7U5_9RHOB        Unreviewed;       542 AA.
AC   A0A2U2C7U5;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:PWE27864.1};
GN   ORFNames=C4N9_14805 {ECO:0000313|EMBL:PWE27864.1};
OS   Pararhodobacter marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pararhodobacter.
OX   NCBI_TaxID=2184063 {ECO:0000313|EMBL:PWE27864.1, ECO:0000313|Proteomes:UP000244940};
RN   [1] {ECO:0000313|EMBL:PWE27864.1, ECO:0000313|Proteomes:UP000244940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIC4N-9 {ECO:0000313|EMBL:PWE27864.1,
RC   ECO:0000313|Proteomes:UP000244940};
RA   Lai Q.Sr., Liu X., Shao Z.;
RT   "Pararhodobacter marina sp. nov., isolated from deep-sea water of the
RT   Indian Ocean.";
RL   Submitted (MAY-2018) 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:PWE27864.1}.
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DR   EMBL; QEYD01000009; PWE27864.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U2C7U5; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000244940; Unassembled WGS sequence.
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   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:UP000244940};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..109
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          191..320
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          395..529
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   542 AA;  58233 MW;  B815444EA196CD29 CRC64;
     MSDTKTYVHQ SIAQAVLDHG ITTMYGLMGD ANLFMVDHYV REGGGQFVPV AYEGSAVLMA
     AAHARISQSV AVATVTHGPA LTNCVTALVE AARAQVPMVL LAGDTAVMAP QNLQNIDQRE
     VVHITGAGFL QMRAPETASY DVAHAFHRAR VEKRPIVLNM PADFMWQEVQ HEACVFPVFG
     APAYVPEGDD LDQAVGMIAS AKRPIVLAGV GALDARDKIV ALAERMEAPL ATTLKAKDLF
     RGHPSNMGIF GTLSTPAAYE AIDKADCIVA FGSSLHHFTT DQGKLLKGKR VVQINSDATA
     AAKNFRPDAV LVSDAGLTAD NIVWWLNEAE IAPTGFAKEL DMDELTRHPV GRPGDTAEGC
     INFVQALERL EKALPENRLV TTDGGRFMTE VWCRISSPDA RSFIATTNFG SIGLGLQVAI
     GAGIAAPDRP VVLFTGDGGF MMGGINEFNT AVRLKQDLIV IVANDNAYGA EHIQFLDRQM
     DPGLAQFEWP SFADVATALG GQGMVVTSDE ELDAAMKAIE TRDKPLLIEL RLDPNDVPRM
     RV
//