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Bacillus subtilis subsp. subtilis str. 168 (bsub0)
Gene : alsS
DDBJ      :alsS         alpha-acetolactate synthase
Swiss-Prot:ILVX_BACSU   RecName: Full=Acetolactate synthase;         EC=2.2.1.6;AltName: Full=Acetohydroxy-acid synthase;AltName: Full=ALS;

Homologs  Archaea  56/68 : Bacteria  759/915 : Eukaryota  178/199 : Viruses  0/175   --->[See Alignment]
c.31.1c.36.1
:570 amino acids
:SECSTR
:PSIPRED
:BLT:PDB   16->549 1ozgA PDBj e-151 51.5 %
:RPS:PDB   16->544 1bfdA PDBj 8e-95 21.4 %
:RPS:SCOP  16->177 1ozfA2  c.36.1.5 * 2e-44 63.6 %
:RPS:SCOP  207->337 1ovmA1  c.31.1.3 * 2e-21 14.6 %
:RPS:SCOP  370->550 1powA3  c.36.1.9 * 8e-35 24.3 %
:HMM:SCOP  3->196 1ybhA2 c.36.1.5 * 5.4e-48 40.8 %
:HMM:SCOP  191->379 1ozhA1 c.31.1.3 * 1e-36 27.4 %
:HMM:SCOP  372->550 2djiA3 c.36.1.9 * 1.9e-57 37.4 %
:RPS:PFM   16->174 PF02776 * TPP_enzyme_N 2e-36 49.0 %
:RPS:PFM   210->332 PF00205 * TPP_enzyme_M 2e-10 31.9 %
:RPS:PFM   410->541 PF02775 * TPP_enzyme_C 3e-23 40.9 %
:HMM:PFM   15->179 PF02776 * TPP_enzyme_N 9.6e-56 46.7 165/172  
:HMM:PFM   396->542 PF02775 * TPP_enzyme_C 1.4e-46 41.8 146/150  
:HMM:PFM   200->333 PF00205 * TPP_enzyme_M 2.4e-25 31.1 132/137  
:BLT:SWISS 1->570 ILVX_BACSU 0.0 100.0 %
:PROS 433->452|PS00187|TPP_ENZYMES
:SEG

SeqInfo AminoSeq See neighboring genes
Links GIB DAD Abbreviations Back to title page
GT:ID CAB15618.2 GT:GENE alsS GT:PRODUCT alpha-acetolactate synthase GT:DATABASE GIB00011CH01 GT:ORG bsub0 GB:ACCESSION GIB00011CH01 GB:LOCATION complement(3709628..3711340) GB:FROM 3709628 GB:TO 3711340 GB:DIRECTION - GB:GENE alsS GB:PRODUCT alpha-acetolactate synthase GB:FUNCTION 16.14: Store 16.11: Scavenge (Catabolism) 16.8: Protect GB:NOTE Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; PubMedId: 10972805, 12363365, 17183216, 7685336; Product type e: enzyme GB:PROTEIN_ID CAB15618.2 GB:DB_XREF GOA:Q04789 HSSP:1JSC InterPro:IPR012000 SubtiList:BG10471 UniProtKB/Swiss-Prot:Q04789 GB:GENE:GENE alsS LENGTH 570 SQ:AASEQ MTKATKEQKSLVKNRGAELVVDCLVEQGVTHVFGIPGAKIDAVFDALQDKGPEIIVARHEQNAAFMAQAVGRLTGKPGVVLVTSGPGASNLATGLLTANTEGDPVVALAGNVIRADRLKRTHQSLDNAALFQPITKYSVEVQDVKNIPEAVTNAFRIASAGQAGAAFVSFPQDVVNEVTNTKNVRAVAAPKLGPAADDAISAAIAKIQTAKLPVVLVGMKGGRPEAIKAVRKLLKKVQLPFVETYQAAGTLSRDLEDQYFGRIGLFRNQPGDLLLEQADVVLTIGYDPIEYDPKFWNINGDRTIIHLDEIIADIDHAYQPDLELIGDIPSTINHIEHDAVKVEFAEREQKILSDLKQYMHEGEQVPADWKSDRAHPLEIVKELRNAVDDHVTVTCDIGSHAIWMSRYFRSYEPLTLMISNGMQTLGVALPWAIGASLVKPGEKVVSVSGDGGFLFSAMELETAVRLKAPIVHIVWNDSTYDMVAFQQLKKYNRTSAVDFGNIDIVKYAESFGATGLRVESPDQLADVLRQGMNAEGPVIIDVPVDYSDNINLASDKLPKEFGELMKTKAL GT:EXON 1|1-570:0| SW:ID ILVX_BACSU SW:DE RecName: Full=Acetolactate synthase; EC=2.2.1.6;AltName: Full=Acetohydroxy-acid synthase;AltName: Full=ALS; SW:GN Name=alsS; OrderedLocusNames=BSU36010; SW:KW Acetoin biosynthesis; Complete proteome; FAD; Flavoprotein; Magnesium;Metal-binding; Thiamine pyrophosphate; Transferase. SW:EXACT T SW:FUNC + BL:SWS:NREP 1 BL:SWS:REP 1->570|ILVX_BACSU|0.0|100.0|570/570| GO:SWS:NREP 3 GO:SWS GO:0045151|"GO:acetoin biosynthetic process"|Acetoin biosynthesis| GO:SWS GO:0046872|"GO:metal ion binding"|Metal-binding| GO:SWS GO:0016740|"GO:transferase activity"|Transferase| PROS 433->452|PS00187|TPP_ENZYMES|PDOC00166| SEG 195->205|aaddaisaaia| BL:PDB:NREP 1 BL:PDB:REP 16->549|1ozgA|e-151|51.5|530/549| RP:PDB:NREP 1 RP:PDB:REP 16->544|1bfdA|8e-95|21.4|514/523| RP:PFM:NREP 3 RP:PFM:REP 16->174|PF02776|2e-36|49.0|157/170|TPP_enzyme_N| RP:PFM:REP 210->332|PF00205|2e-10|31.9|119/138|TPP_enzyme_M| RP:PFM:REP 410->541|PF02775|3e-23|40.9|132/139|TPP_enzyme_C| HM:PFM:NREP 3 HM:PFM:REP 15->179|PF02776|9.6e-56|46.7|165/172|TPP_enzyme_N| HM:PFM:REP 396->542|PF02775|1.4e-46|41.8|146/150|TPP_enzyme_C| HM:PFM:REP 200->333|PF00205|2.4e-25|31.1|132/137|TPP_enzyme_M| GO:PFM:NREP 5 GO:PFM GO:0030976|"GO:thiamin pyrophosphate binding"|PF02776|IPR012001| GO:PFM GO:0000287|"GO:magnesium ion binding"|PF00205|IPR012000| GO:PFM GO:0030976|"GO:thiamin pyrophosphate binding"|PF00205|IPR012000| GO:PFM GO:0003824|"GO:catalytic activity"|PF02775|IPR011766| GO:PFM GO:0030976|"GO:thiamin pyrophosphate binding"|PF02775|IPR011766| RP:SCP:NREP 3 RP:SCP:REP 16->177|1ozfA2|2e-44|63.6|162/178|c.36.1.5| RP:SCP:REP 207->337|1ovmA1|2e-21|14.6|130/161|c.31.1.3| RP:SCP:REP 370->550|1powA3|8e-35|24.3|181/228|c.36.1.9| HM:SCP:REP 3->196|1ybhA2|5.4e-48|40.8|191/0|c.36.1.5|1/2|Thiamin diphosphate-binding fold (THDP-binding)| HM:SCP:REP 191->379|1ozhA1|1e-36|27.4|179/179|c.31.1.3|1/1|DHS-like NAD/FAD-binding domain| HM:SCP:REP 372->550|2djiA3|1.9e-57|37.4|179/0|c.36.1.9|1/1|Thiamin diphosphate-binding fold (THDP-binding)| OP:NHOMO 3048 OP:NHOMOORG 993 OP:PATTERN 11-1--5554455563-31221143--21122243222222221312213343211-----2421-11 4372932222223255844-43225C444445255554DB1223133-222174854311535145A76521222111-211711111223112--111-1111142211---------------21111111111222331111734523322211113111222333721111111111111211111-133444443461454435334434444225242-3333432523333333333333323333122145112-27622553331343231111---22222222222222-------------211222111122125-------4-321331---112--2122165222121221112--1-111112-11-134CA92148357633333332316-66955B49562-2443357665786412157942346575555555532112332-----------------------------3325226C9888899987555599CD88885696F677724544233227344B63333111311111111112422-922212234233412213112433323352521111111111-1-------1111211322231312222332422322222322233-1-311111111145542545666576766-6646766656666665664878553245455545555555553765666651-64444443444411---1---111122741222212-22212112222221312432888847454588631123----1---313253333322222332222222211111111331132-------------------------------------11--1-111122 ----22--------174214443866733333333323232333443424335222321322211212-1231112212221111123-11142111111211222-24-42322221-1222124262AK2-42412212-252122122-1421123364163211122234111118112235125123213111- ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- STR:NPRED 566 STR:RPRED 99.3 SQ:SECSTR ####cccccTTccEEHHHHHHHHHHHTTccEEEEcccGGGHHHHTTccTHTcEEEEcccHHHHHHHHHHHHHHHTccEEEEEEHHHHHHHTHHHHHHHHHHTccEEEEEEEccHHHHTTTcTccTTGGGTTTTcccEEEccccGGGHHHHHHHHHHHHHccccccEEEEEEGGGTTccccGGGGGGTTccccccccccHHHHHHHHHHHccccEEEEcHHHHHHTcHHHHHHHHHHHTccEEEccccccccccTTcTTEEEEccccGHHHHHHHHTTccEEEEEcccTTccccccccccTTcEEEEEEccHHHHHHccccEEEEEccHHHHHHHHHHHcccccccccccccHHHHHHHHHHHcccccccccccccHHHHHHHHHHHccTTcEEEEEcGGGHHHHHHHcccccTTcEEEEcTTcccccHHHHHHHHHHHcTTccEEEEEEHHHHTTTGGGHHHHHHHTcccEEEEEEccccHHHHHHHHHTTccccccccccccHHHHHHHTTcEEEEEccHHHHHHHHHHHHHccccEEEEEEccTTccccccccGGccHHHHHHHHTTc PSIPRED cccccHHHHHHHHccHHHHHHHHHHHccccEEEEccccccHHHHHHHHHcccEEEEEccHHHHHHHHHHHHHHcccEEEEEEcccHHHHHHHHHHHHHHHHcccEEEEcccccHHHccccccccccHHHHHHHcccEEEEcccHHHHHHHHHHHHHHHHcccccEEEEEcccHHHcccccccccccccccccccccHHHHHHHHHHHHcccccEEEEEcccccHHHHHHHHHHHHHHcccEEEcccccccccccccccEEEcccccccHHHHHHHHHccEEEEEcccccccccccccccccccEEEEEccHHHcccccccccEEEEcHHHHHHHHHHHHccccccccHHHHHHHHHHHHHHHHHcccccccccccHHHHHHHHHHHcccccEEEEccccHHHHHHHHcccccccEEEEccccccccHHHHHHHHHHHHccccEEEEEEEcHHHcccHHHHHHHHHccccEEEEEEEcccccHHcccHHcccccccccccccccHHHHHHHcccEEEEEccHHHHHHHHHHHHHccccEEEEEEcccccccccHHHHccHHHHHHHHcccc //