ILVB_KLEPN
ID ILVB_KLEPN Reviewed; 559 AA.
AC P27696;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Acetolactate synthase, catabolic;
DE Short=ALS;
DE EC=2.2.1.6;
GN Name=budB; Synonyms=ilvK;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1644303; DOI=10.1016/0378-1119(92)90500-o;
RA Peng H.-L., Wang P.-Y., Wu C.-M., Hwang D.-C., Chang H.-Y.;
RT "Cloning, sequencing and heterologous expression of a Klebsiella pneumoniae
RT gene encoding an FAD-independent acetolactate synthase.";
RL Gene 117:125-130(1992).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=14557277; DOI=10.1074/jbc.m304038200;
RA Pang S.S., Duggleby R.G., Schowen R.L., Guddat L.W.;
RT "The crystal structures of Klebsiella pneumoniae acetolactate synthase with
RT enzyme-bound cofactor and with an unusual intermediate.";
RL J. Biol. Chem. 279:2242-2253(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2;
CC Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.;
CC -!- PATHWAY: Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-
CC butane-2,3-diol from pyruvate: step 1/3.
CC -!- MISCELLANEOUS: Does not seem to require thiamine pyrophosphate.
CC -!- MISCELLANEOUS: Valine resistant.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; M73842; AAA25079.1; -; Genomic_DNA.
DR PIR; JC1218; JC1218.
DR PDB; 1OZF; X-ray; 2.30 A; A/B=1-559.
DR PDB; 1OZG; X-ray; 2.30 A; A/B=1-559.
DR PDB; 1OZH; X-ray; 2.00 A; A/B/C/D=1-559.
DR PDB; 5D6R; X-ray; 2.28 A; B/M=1-559.
DR PDB; 5DX6; X-ray; 1.75 A; A/B=1-559.
DR PDB; 5WDG; X-ray; 2.12 A; A/B=1-559.
DR PDBsum; 1OZF; -.
DR PDBsum; 1OZG; -.
DR PDBsum; 1OZH; -.
DR PDBsum; 5D6R; -.
DR PDBsum; 5DX6; -.
DR PDBsum; 5WDG; -.
DR AlphaFoldDB; P27696; -.
DR SMR; P27696; -.
DR DrugBank; DB03361; 2-{(9as)-9a-[(1s)-1-Hydroxyethyl]-2,7-Dimethyl-9a,10-Dihydro-5h-Pyrimido[4,5-D][1,3]Thiazolo[3,2-a]Pyrimidin-8-Yl}Ethyl Trihydrogen Diphosphate.
DR DrugBank; DB01987; Cocarboxylase.
DR DrugBank; DB02327; Triethylene glycol.
DR BioCyc; MetaCyc:MON-15237; -.
DR UniPathway; UPA00626; UER00677.
DR EvolutionaryTrace; P27696; -.
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 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-bd_C.
DR PANTHER; PTHR18968; PTHR18968; 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; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR02418; acolac_catab; 1.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Magnesium; Metal-binding;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..559
FT /note="Acetolactate synthase, catabolic"
FT /id="PRO_0000090797"
FT BINDING 159
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 263..284
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 304..323
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT STRAND 1..5
FT /evidence="ECO:0007829|PDB:5WDG"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 57..71
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 111..115
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 124..128
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:5DX6"
FT TURN 243..246
FT /evidence="ECO:0007829|PDB:5DX6"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 267..274
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 276..282
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 298..306
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 324..333
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 343..360
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:1OZH"
FT HELIX 373..383
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 396..403
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 411..414
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 425..435
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 447..453
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 456..463
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 467..473
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 478..488
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 501..506
FT /evidence="ECO:0007829|PDB:5DX6"
FT TURN 507..509
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 510..514
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 518..520
FT /evidence="ECO:0007829|PDB:1OZH"
FT HELIX 521..530
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:5DX6"
FT STRAND 535..541
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 546..550
FT /evidence="ECO:0007829|PDB:5DX6"
FT HELIX 555..557
FT /evidence="ECO:0007829|PDB:5DX6"
SQ SEQUENCE 559 AA; 60338 MW; 7775373ABEEE603D CRC64;
MDKQYPVRQW AHGADLVVSQ LEAQGVRQVF GIPGAKIDKV FDSLLDSSIR IIPVRHEANA
AFMAAAVGRI TGKAGVALVT SGPGCSNLIT GMATANSEGD PVVALGGAVK RADKAKQVHQ
SMDTVAMFSP VTKYAIEVTA PDALAEVVSN AFRAAEQGRP GSAFVSLPQD VVDGPVSGKV
LPASGAPQMG AAPDDAIDQV AKLIAQAKNP IFLLGLMASQ PENSKALRRL LETSHIPVTS
TYQAAGAVNQ DNFSRFAGRV GLFNNQAGDR LLQLADLVIC IGYSPVEYEP AMWNSGNATL
VHIDVLPAYE ERNYTPDVEL VGDIAGTLNK LAQNIDHRLV LSPQAAEILR DRQHQRELLD
RRGAQLNQFA LHPLRIVRAM QDIVNSDVTL TVDMGSFHIW IARYLYTFRA RQVMISNGQQ
TMGVALPWAI GAWLVNPERK VVSVSGDGGF LQSSMELETA VRLKANVLHL IWVDNGYNMV
AIQEEKKYQR LSGVEFGPMD FKAYAESFGA KGFAVESAEA LEPTLRAAMD VDGPAVVAIP
VDYRDNPLLM GQLHLSQIL
