ID I4WJD4_9GAMM Unreviewed; 486 AA.
AC I4WJD4;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:EIL99575.1};
DE Flags: Fragment;
GN ORFNames=UU5_02722 {ECO:0000313|EMBL:EIL99575.1};
OS Rhodanobacter sp. 115.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1162282 {ECO:0000313|EMBL:EIL99575.1, ECO:0000313|Proteomes:UP000004557};
RN [1] {ECO:0000313|EMBL:EIL99575.1, ECO:0000313|Proteomes:UP000004557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=115 {ECO:0000313|EMBL:EIL99575.1,
RC ECO:0000313|Proteomes:UP000004557};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
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:EIL99575.1}.
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DR EMBL; AJXS01000074; EIL99575.1; -; Genomic_DNA.
DR RefSeq; WP_008208906.1; NZ_AJXS01000074.1.
DR AlphaFoldDB; I4WJD4; -.
DR PATRIC; fig|1162282.3.peg.526; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000004557; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; 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 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}.
FT DOMAIN 1..55
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 128..259
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 318..463
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EIL99575.1"
SQ SEQUENCE 486 AA; 53884 MW; A09C9DA38C9A5CA7 CRC64;
GEAGVALSTL GPGATNLVTA AAYAQLGAMP MLMITGQKPI RTHKQGLFQL VDVVDMMQPL
TKYTRQLVSA PTIPARVREA FRRAEEERPG AVHLELPEDI ARDDVGDAIL LPTEYARRPS
ADDAALVQAA EAISAARHPI LMIGAAANRQ RTAVALRDFI DKLGIPFFTT QMGKGVVDED
HPLWLGNAAL SDGDFVHRAI DAADVIINAG HDVVEKPPFF MRKGRRTVIH INFASAEVDT
VYFPQIEVVG DIAHTIERLT DALQPQKHWN FDYFDKVRHA FHEQLQEHAD DARFPMHPVR
IVADTRRAMP DDGVLCLDNG MYKLWYARYY RARQPNTVLL DNALATMGAG LPSAMAAKMV
FPERKVLAIC GDGGFMMNAQ ELETAVRLKL DLVILLLRDD AYGMIRWKQA EMRHADYGMQ
FGNPDFVMFA EAHGAHGHRP ACADEFLPTL QQAYAQGGVH LIDLAIDYAD NHRILDEQIR
QLSAAV
//
