ID A0A0P0N5H5_9CREN Unreviewed; 582 AA.
AC A0A0P0N5H5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591};
DE EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591};
GN ORFNames=Pdsh_03865 {ECO:0000313|EMBL:OWJ55200.1}, Pyrde_1930
GN {ECO:0000313|EMBL:ALL01973.1};
OS Pyrodictium delaneyi.
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Pyrodictium.
OX NCBI_TaxID=1273541 {ECO:0000313|EMBL:ALL01973.1, ECO:0000313|Proteomes:UP000058613};
RN [1] {ECO:0000313|EMBL:ALL01973.1, ECO:0000313|Proteomes:UP000058613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Su06 {ECO:0000313|EMBL:ALL01973.1,
RC ECO:0000313|Proteomes:UP000058613};
RA Jung J.-H., Lin J., Holden J.F., Park C.-S.;
RT "Complete genome sequence of hyperthermophilic archaeon Pyrodictium
RT delaneyi Su06.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OWJ55200.1, ECO:0000313|Proteomes:UP000196694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hulk {ECO:0000313|EMBL:OWJ55200.1,
RC ECO:0000313|Proteomes:UP000196694};
RA Demey L.M., Miller C., Manzella M., Reguera G., Kashefi K.;
RT "The draft genome of the hyperthermophilic archaeon 'Pyrodictium delaneyi
RT strain Hulk', an iron and nitrate reducer, reveals the capacity for sulfate
RT reduction.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|RuleBase:RU003591};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-oxocarboxylate + CoA + 2 oxidized [2Fe-2S]-[ferredoxin] =
CC an acyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:42316, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:35179, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58342; EC=1.2.7.11;
CC Evidence={ECO:0000256|ARBA:ARBA00000005};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU003591};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU003591};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|RuleBase:RU003591};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000256|RuleBase:RU003591};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004974, ECO:0000256|RuleBase:RU003591}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025,
CC ECO:0000256|RuleBase:RU003591}.
CC -!- SUBUNIT: Heterodimer composed of an alpha and a beta subunit.
CC {ECO:0000256|ARBA:ARBA00011631}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU003591}.
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DR EMBL; CP013011; ALL01973.1; -; Genomic_DNA.
DR EMBL; NCQP01000002; OWJ55200.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P0N5H5; -.
DR STRING; 1273541.Pyrde_1930; -.
DR KEGG; pdl:Pyrde_1930; -.
DR PATRIC; fig|1273541.4.peg.2051; -.
DR OrthoDB; 6837at2157; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000058613; Chromosome.
DR Proteomes; UP000196694; Unassembled WGS sequence.
DR GO; GO:0018491; F:2-oxobutyrate synthase activity; IEA:UniProt.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProt.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02015; TPP_AHAS; 1.
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; IPR012846; Acetolactate_synth_lsu.
DR InterPro; IPR039368; AHAS_TPP.
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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR00118; acolac_lg; 1.
DR PANTHER; PTHR18968:SF169; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU003591};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|RuleBase:RU003591}; Magnesium {ECO:0000256|RuleBase:RU003591};
KW Metal-binding {ECO:0000256|RuleBase:RU003591};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591}.
FT DOMAIN 3..113
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..325
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 386..534
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 582 AA; 64030 MW; D13E50C14B06ADA4 CRC64;
MVDHIARILK DLSATQVFGV TGGSIMGLFD ALALEDFEIY MFRHEQGAAH AADAYGRIAR
RPGIALATSG PGATNLVTGI ANAYFDSAPM VAITGQVPTS VFGRDAFQET DIVGVTAPIT
KFAYQVKKPE EAGPAIRTAY RLAVEGRPGP TLVDLPRDVQ LTKYEPRDEP EYLPIDFAKY
QPPSPDPEAV RRAARLLLAA SRPVILVGTG VYWSGATAEV IELAERLQAP IVTTLPGKNA
VPADHPLVMG PAGMHGRAEA DAALANADVI LAVGTRFSDR TVGRFEPELR EKKIIHIDID
PSEHGKNVPP AVSIIADARE ALQAILREMP AVPQRDKRFI EWLLWIRRRY EDAMEKLAAR
MRKFAPWKVL KTLRQAVPRN TITVTGVGSH QMWSEIHWDV YVPGTWVTSA GLGTMGFCIP
AALGAKIAAR DRPVLCIDGD GSFQMTMNNL ALVRDYDLPI IVTVFDNRAL MLVKQWQIFL
YDRRIVATEY SQWPDFTKIA EAYGIEAIRP ASLEEIDTAV RRAIRNNEPL IVVVDIDNNE
DIVLPWVKPG EWLTDAILPP GMEDVSLVFR EEKLAAAPAA GR
//