ID A0A0D5M037_9GAMM Unreviewed; 615 AA.
AC A0A0D5M037;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:AJY49093.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:AJY49093.1};
GN ORFNames=KO116_00594 {ECO:0000313|EMBL:AJY49093.1};
OS Halomonas sp. KO116.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1504981 {ECO:0000313|EMBL:AJY49093.1, ECO:0000313|Proteomes:UP000028645};
RN [1] {ECO:0000313|EMBL:AJY49093.1, ECO:0000313|Proteomes:UP000028645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KO116 {ECO:0000313|EMBL:AJY49093.1,
RC ECO:0000313|Proteomes:UP000028645};
RX PubMed=25953187;
RA O'Dell K.B., Woo H.L., Utturkar S., Klingeman D., Brown S.D., Hazen T.C.;
RT "Genome Sequence of Halomonas sp. Strain KO116, an Ionic Liquid-Tolerant
RT Marine Bacterium Isolated from a Lignin-Enriched Seawater Microcosm.";
RL Genome Announc. 3:0-0(2015).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP011052; AJY49093.1; -; Genomic_DNA.
DR RefSeq; WP_035560689.1; NZ_CP011052.1.
DR AlphaFoldDB; A0A0D5M037; -.
DR STRING; 1504981.KO116_00594; -.
DR KEGG; hak:KO116_00594; -.
DR eggNOG; COG3962; Bacteria.
DR HOGENOM; CLU_013748_6_0_6; -.
DR OrthoDB; 3194735at2; -.
DR Proteomes; UP000028645; Chromosome.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR GO; GO:0019310; P:inositol catabolic process; IEA:InterPro.
DR CDD; cd02003; TPP_IolD; 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; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR030817; Myo_inos_IolD.
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; TIGR04377; myo_inos_iolD; 1.
DR PANTHER; PTHR18968:SF9; 3D-(3,5/4)-TRIHYDROXYCYCLOHEXANE-1,2-DIONE HYDROLASE; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:AJY49093.1}.
FT DOMAIN 7..131
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 220..345
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 417..569
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 615 AA; 65751 MW; 74724AFF42A01ED0 CRC64;
MSTIRLTMAQ ALVKYLAAQR IEVDGQEVAL FEGVFAIFGH GNVAGMGEAL YHVQDTLPTF
RAHNEQAMAH AAIAFAKANN RQRLMAATSS IGPGATNMVT AAALAHANRL PILLLPGDTF
ATREPDPVLQ QVEHFGDPTI SVNDCFRPVS RYFDRINRPE QLLTSLPQAL ATLLDPEHCG
PATLALPQDV QTFAYDYPEA FFAPKVHRIR RPPPDFYELR QAVAALQQAK RPLIITGGGV
HYASACDALA EFAKARGIPV AETQAGKGAL ADSHPCAVGA IGVTGSAAAN QLAEQADVIL
AVGTRLQDFT TGSRALFEGS EKTLIALNVG RFDSLKHQAL PLSCDALVGL GQLDAALGEW
RGSDEWREQT GTLKREWVEI VHNVTADQGL ALPTDAQVIG AVNRQAGNDT TVVCAAGGLP
GELHKLWQCS GPGSYHVEYG FSCMGYEIAG GLGVKMAKPD NEVVVMVGDG SYLMHNSELA
TSVMLGHKLI VVVLDNRGYG CINRLQQATG GAGFNNLLQD CRTVEAGAPK TDFAAHAKAL
GCESESVTGI AELEQALVRA RSATSTYVIA LDTDPLPSTQ EGGAWWEVAV PEVSEREAVN
KAYQGYRKAK QRQRH
//