ID A0A085JCS8_9GAMM Unreviewed; 558 AA.
AC A0A085JCS8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Acetolactate synthase, catabolic {ECO:0000313|EMBL:KFD18274.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:KFD18274.1};
GN Name=alsS {ECO:0000313|EMBL:KFD18274.1};
GN ORFNames=GTPT_2464 {ECO:0000313|EMBL:KFD18274.1};
OS Tatumella ptyseos ATCC 33301.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Tatumella.
OX NCBI_TaxID=1005995 {ECO:0000313|EMBL:KFD18274.1, ECO:0000313|Proteomes:UP000028602};
RN [1] {ECO:0000313|EMBL:KFD18274.1, ECO:0000313|Proteomes:UP000028602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33301 {ECO:0000313|EMBL:KFD18274.1,
RC ECO:0000313|Proteomes:UP000028602};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-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:KFD18274.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JMPR01000038; KFD18274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085JCS8; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000028602; 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 GO; GO:0034077; P:butanediol metabolic process; 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; IPR012782; Acetolactate_synth_catblc.
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 NCBIfam; TIGR02418; acolac_catab; 1.
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:UP000028602};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:KFD18274.1}.
FT DOMAIN 13..127
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 392..537
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 558 AA; 60379 MW; 884E29849B85ED75 CRC64;
MNKSDKKTEW KCGADLVVAQ LEEQQVKYVF GIPGAKIDRV FDSLEDSSII TVPVRLEANA
GFMAGAIGRL TGKAGVALVT SGPGCSNLIT SAATATSEGD PFVAIGGAVS RQDHLKQVHQ
TMDTVSMFRP VTKYSAEVTS SSAIAEVLSN GFRAAEFGRP GASFISLPMD IVNEPANGHV
LSARLPSLGT APQQEINEVS ALIAQAKNPV LLLGLMASQP RNADAVRRLL TRSEIPVTST
YQAAGVIDQN HFSRFAGRVG LFNNQAGDQL LRNADLIITV GYSPVEYEPV KWNQGTARLV
HIDVLPAETD SHYSPDIELI GDIAGTVDLL AEQINHRYAL SHSTTLILQE RQQQRELLAQ
KGRSLQQFAI HPLRLVRAMQ DIVNSDVTLC VDMGSFHIWI ARYLYSFRAR QVLISNGQQT
MGVALPWAIG AALVDPQRKV VSVSGDGGFM QSSMELETAV RLGVNILHII WVDNCYNMVA
IQEEKKYNRA SGVDFGPIDF KAYAEAFGAK GFAVTSSETL ESTLRAAMDV QGPAVVAIPV
DYSANALLMS QLNMAEMF
//
