ID C6KIX7_9STRA Unreviewed; 582 AA.
AC C6KIX7;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Acetolactate synthase {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145, ECO:0000256|RuleBase:RU003591};
GN Name=ilvB {ECO:0000313|EMBL:ACS36933.1};
GN ORFNames=AulaCp045 {ECO:0000313|EMBL:ACS36933.1};
OS Aureoumbra lagunensis.
OG Plastid; Chloroplast {ECO:0000313|EMBL:ACS36933.1}.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Pelagophyceae; Pelagomonadales;
OC Aureoumbra.
OX NCBI_TaxID=44058 {ECO:0000313|EMBL:ACS36933.1};
RN [1] {ECO:0000313|EMBL:ACS36933.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP 1507 {ECO:0000313|EMBL:ACS36933.1};
RX AGRICOLA=IND44379834; DOI=10.1111/j.1529-8817.2010.00841.x;
RA Ong H.C., Wilhelm S.W., Gobler C.J., Bullerjahn G., Jacobs M.A., McKay J.,
RA Sims E.H., Gillett W.G., Zhou Y., Haugen E., Rocap G., Cattolico R.A.;
RT "Analyses of the complete chloroplast genome sequences of two members of
RT the pelagophyceae: Aureococcus anophagefferens CCMP1984 and Aureoumbra
RT lagunensis CCMP1507.";
RL J. Phycol. 46:602-615(2010).
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 -!- 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 -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU003591}.
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DR EMBL; GQ231542; ACS36933.1; -; Genomic_DNA.
DR RefSeq; YP_003002221.1; NC_012903.1.
DR AlphaFoldDB; C6KIX7; -.
DR GeneID; 8097424; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
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: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; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR NCBIfam; TIGR00118; acolac_lg; 1.
DR PANTHER; PTHR18968:SF13; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
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}; Chloroplast {ECO:0000313|EMBL:ACS36933.1};
KW Magnesium {ECO:0000256|RuleBase:RU003591};
KW Metal-binding {ECO:0000256|RuleBase:RU003591};
KW Plastid {ECO:0000313|EMBL:ACS36933.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW Transferase {ECO:0000256|RuleBase:RU003591}.
FT DOMAIN 5..121
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 201..334
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 399..549
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 582 AA; 64284 MW; F444F7980FC3B10E CRC64;
MKKRGSFSLL DSLVRNGTEY IFGYPGGAIL PIYDELYKWE QKKLINHILV RHEQGAVHAA
DGYARATGKV GVCFATSGPG ATNLVTGIAT AQMDSIPLLV ITGQVGRAFI GTDAFQETDI
FGITLPIVKH SYVVRDVTKI SSIVSEAFYL ARNGRPGPVL IDIPKDVGLE EFSNYTPVNQ
NTIIQSKGFR FSYRSTKKRL SQVFDLIMES SQPLLYVGGG VIAANAHNEL LELAEHFKIP
VTTTLMGKGA FDETNSLALG MLGMHGTAYA NFSVSECDLL IAVGARFDDR VTGKLDEFAV
NAQVIHIDID PAEVGKNRQP NISLVGDVKK ILSEFLRLVK SRKNLYNADH TFTWCQRISK
WQNTYPLQIP DQNNNNSLSP QKILTTLNKI APDALFTTDV GQHQMWSAQF LKCQPRKWSS
SAGLGTMGYG LPAAIGNQIA FPDQLVICIT GDASIQMNIQ ELGTIAQYNL PIKIILLNNK
WQGMVRQWQQ SFYGERYSHS SMQQGMPDFV QLANAYDISG KVLIPNEDMD LEQELIDIVN
TPGPCFIDCQ ITKDENCYPM VAPGKSNAQM IGILKQNTVD VK
//
