ID A0A0B0EG08_9BACT Unreviewed; 546 AA.
AC A0A0B0EG08;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:KHE91001.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:KHE91001.1};
GN Name=ilvX {ECO:0000313|EMBL:KHE91001.1};
GN ORFNames=SCABRO_03303 {ECO:0000313|EMBL:KHE91001.1};
OS Candidatus Scalindua brodae.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Scalinduaceae; Scalindua.
OX NCBI_TaxID=237368 {ECO:0000313|EMBL:KHE91001.1, ECO:0000313|Proteomes:UP000030652};
RN [1] {ECO:0000313|EMBL:KHE91001.1, ECO:0000313|Proteomes:UP000030652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU1 {ECO:0000313|EMBL:KHE91001.1};
RA Speth D.R., Russ L., Kartal B., Op den Camp H.J., Dutilh B.E., Jetten M.S.;
RT "Draft genome of anammox bacterium scalindua brodae, obtained using
RT differential coverage binning of sequence data from two enrichment
RT reactors.";
RL Submitted (OCT-2014) 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:KHE91001.1}.
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DR EMBL; JRYO01000225; KHE91001.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B0EG08; -.
DR PATRIC; fig|237368.3.peg.3567; -.
DR eggNOG; COG0028; Bacteria.
DR Proteomes; UP000030652; 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; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:KHE91001.1}.
FT DOMAIN 1..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 186..318
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 378..523
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 546 AA; 60850 MW; 8977BD55F5F9963C CRC64;
MKASDLFVKA LENEGVEYVF GIPGEENLDF LNSLKDSKIK LILTRHEQGA GFMAATVGRL
TGKPGVCLAT LGPGATNLVT PAAYANLGAM PMLMITGQKP IMKSKQGRFQ IIDTVDMMRP
ITKYSRQIVN GNSIPSMTRE ACRIAQEERP GAVHLELPED IAAEECVDRL FEVVGYRRPD
ADDLDISKAV RMIEEAKMPL ILIGAGANRK RTSKALRKLI ETTQIPYFTT QMGKGVVDAR
HPQCLGTAAL SDNDFLHCAI SRADLIINIG HDVIEKPPFF MTDRQKVIHV NFFPANVDDV
YFPQLIVVGD IATSVEHLAR HLKEKNANWD FSYFKRIQEN VKEHLSKYFE DNRFPILPQR
VVYIVRKQLP EDGIVTLDNG VYKIWFARNY RCYHPNTLLL DNALATMGAG LASAIAAKMI
KPDKKVIAVC GDGGFLMNSQ ELETAVRLGL DLTIIILDDG GYGMIKWKQE GMGFDNFGLD
YSNPDFVKYA ESYGATGYRP DSVQSFEDVL EKSLNTHGVH IIDLAVDYSL NHSILNVLLK
EKTCIL
//
