ID A0A132BX55_9RHOB Unreviewed; 537 AA.
AC A0A132BX55;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KUP92330.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:KUP92330.1};
GN Name=alsS {ECO:0000313|EMBL:KUP92330.1};
GN ORFNames=TRIHO_28180 {ECO:0000313|EMBL:KUP92330.1};
OS Tritonibacter horizontis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tritonibacter.
OX NCBI_TaxID=1768241 {ECO:0000313|EMBL:KUP92330.1, ECO:0000313|Proteomes:UP000068382};
RN [1] {ECO:0000313|EMBL:KUP92330.1, ECO:0000313|Proteomes:UP000068382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O3.65 {ECO:0000313|EMBL:KUP92330.1,
RC ECO:0000313|Proteomes:UP000068382};
RA Poehlein A., Giebel H.A., Voget S., Brinkhoff T.;
RT "Genome sequence of the marine Rhodobacteraceae strain O3.65, Candidatus
RT Tritonibacter horizontis.";
RL Submitted (DEC-2015) 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:KUP92330.1}.
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DR EMBL; LPUY01000076; KUP92330.1; -; Genomic_DNA.
DR RefSeq; WP_068244900.1; NZ_LPUY01000076.1.
DR AlphaFoldDB; A0A132BX55; -.
DR PATRIC; fig|1768241.3.peg.2951; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000068382; 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:SF129; ACETOLACTATE SYNTHASE; 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:UP000068382};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KUP92330.1}.
FT DOMAIN 6..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..325
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 380..525
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 537 AA; 56627 MW; 4B1671F091F19526 CRC64;
MTDPLRAADV LARRLYAAGC RHAFGMPGGE VLTLVDALQR AGITFHLAKH ENCAGFMGEG
VHHADGAPAI LVATLGPGAL NGVNVVANAH QDRVPMLVLT GCVDADEAQT YTHQVLDQQA
VFAPITKASF RLDAAAAEVI ADKSVAIALD PRQGPVHIDV PITVANAPAT ERNIRRAPAG
ATAPAGATLA QAHRWLAEAR RPLAIVGLDA LLPGAPEATR AFLEARQIPF VTTYKAKGIL
PEDHPLCLGG AGLSPLADTH LLPLVESADL ILCIGYDPIE MRPGWREAWD PHSTRVIDIA
PEPNTHYMHQ ASLTLGSALP DTLAALAVAP PSPPPWPEGE IDRSKAALAA AFPRSDAWGP
AGVIAECIDQ LPADTLLTAD SGAHRILLSQ MWTCTAPRQL VQSSGLCTMG CALPLAIGRK
LAQPDRTVVS FSGDAGFLMV AGELATAAEM GLTPIFVVFV DASLALIDLK QRQRQLPNAG
VDFGRHDYAA IGRAFGGAGH RVHNRDELRA ALTAAQQADT FTVIAAEIDR EEYDGRI
//
