ID Q607C4_METCA Unreviewed; 553 AA.
AC Q607C4;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:AAU91941.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:AAU91941.1};
GN Name=ilvK {ECO:0000313|EMBL:AAU91941.1};
GN OrderedLocusNames=MCA1837 {ECO:0000313|EMBL:AAU91941.1};
OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylococcus.
OX NCBI_TaxID=243233 {ECO:0000313|EMBL:AAU91941.1, ECO:0000313|Proteomes:UP000006821};
RN [1] {ECO:0000313|EMBL:AAU91941.1, ECO:0000313|Proteomes:UP000006821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath
RC {ECO:0000313|Proteomes:UP000006821};
RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT "Genomic insights into methanotrophy: the complete genome sequence of
RT Methylococcus capsulatus (Bath).";
RL PLoS Biol. 2:1616-1628(2004).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; AE017282; AAU91941.1; -; Genomic_DNA.
DR RefSeq; WP_010961089.1; NC_002977.6.
DR AlphaFoldDB; Q607C4; -.
DR STRING; 243233.MCA1837; -.
DR KEGG; mca:MCA1837; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_2_6; -.
DR Proteomes; UP000006821; Chromosome.
DR GO; GO:0005948; C:acetolactate synthase complex; ISS:JCVI.
DR GO; GO:0003984; F:acetolactate synthase activity; ISS:JCVI.
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:0006113; P:fermentation; ISS:JCVI.
DR GO; GO:0009097; P:isoleucine biosynthetic process; ISS:JCVI.
DR GO; GO:0009099; P:valine biosynthetic process; ISS:JCVI.
DR CDD; cd02010; TPP_ALS; 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; 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:UP000006821};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:AAU91941.1}.
FT DOMAIN 9..113
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 387..533
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 553 AA; 58952 MW; 1F84A3079FB8B2CB CRC64;
MRETIPPRTG ADLLVDSLQA LGVEYVFGVP GGAILPILNV LADRGPRFIV CRDETGAAFM
AQSWGRITGR PGVVLTTSGP GLINAVCGVA TATEDRDPLV VITGQVPRAV QFKQSHMNLD
SVGLFAPITK WSVEVEEPNT VSEILVNAFR TAQTPCAGAV HVSVPNDMLT APVTAQALAP
AEPAVWGTAP AAVVERAASL LNDAKAPAIL LGLRASTPGA AAAVRRFLER HPLPVAMTFE
AAGTLSRDLV DQFVGRVGYV LNQPGDEVLR QADLVLTIGY DPIEYEPSAW ISPQSQAIHL
DALPAAVDRA YHPAAELVGD IAANLAALGS LLRIEDRAGR PAVAAARRRL LEEQARGAAL
TGMPIHPLRF IHDLRATLDD EATVTCDVGA HEIWMARYFF CYAPRHLLFS MGHQTMGVAL
PWAIGAALAR PGKKVVSVSG DGSFLMTCME LETAVRLKLP IVHIVWKDGG YNLIHSLQMR
DYGRSFGAEF GPTDFVKLAE AFGAIGYRIE SADGIVPVLN RALAADAPVL IEVPIDYSDN
VHLVEAIDAS AQH
//
