ID A0A0D5LZ87_9GAMM Unreviewed; 601 AA.
AC A0A0D5LZ87;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:AJY49474.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:AJY49474.1};
GN ORFNames=KO116_00977 {ECO:0000313|EMBL:AJY49474.1};
OS Halomonas sp. KO116.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1504981 {ECO:0000313|EMBL:AJY49474.1, ECO:0000313|Proteomes:UP000028645};
RN [1] {ECO:0000313|EMBL:AJY49474.1, ECO:0000313|Proteomes:UP000028645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KO116 {ECO:0000313|EMBL:AJY49474.1,
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; AJY49474.1; -; Genomic_DNA.
DR RefSeq; WP_035555781.1; NZ_CP011052.1.
DR AlphaFoldDB; A0A0D5LZ87; -.
DR STRING; 1504981.KO116_00977; -.
DR KEGG; hak:KO116_00977; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_6; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000028645; Chromosome.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
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 CDD; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 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; IPR047211; POXB-like.
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; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 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:AJY49474.1}.
FT DOMAIN 4..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 200..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..544
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 601 AA; 65645 MW; D7647F5C1C4EF52F CRC64;
MTQEVSDFII DRLKQWKVSH IFGYSGDGNN GLMGALNRAD DSITFVQPRH EEMAAFMACG
YAKYTGEVGV CMATSGPGAI HLLNGLYDAK KDHIPVVAIV GQQARTALGG EYQQEVDLVS
LFKDVAGDFV HLATSPGQVR HLIDRAMRIA AGERTVTAIV VPNDLQSQKA VEIPAHAHGT
VHSGVGYTSA NVIPDEHSLA HAADILNAGE RVAILVGAGA RGAEREVEEV ATRLGAGVAK
ALLGRDVLPD DLPYVTGSIG LLGTNPSWTL MAECDTLLMI GSSFPYSEFL PPEGQASGVQ
IDIEPRMLSM RYPMDVNLTG DTRLTLQALI PLLTHKSNRD WQQAIEADVA EWWELLRERA
MGDAHPINPQ RVFWEASQRL PDRCLLSCDS GSATNWYARD LKFRTGMRGS VSGGLATMGN
AVPYAIAAKF AYPERVSIAF VGDGAMQMSG NAELLTIGKY WKRWDDPRLI VIVLNNRDLN
QVTWEMRVQD GDPKYEASQD LPDFSYAQYA DLVGLKGIEV TDPEQIGSAW DQAIANHCPT
VIDFHTDPDI PPIPPHISKQ QAKAYMSAML HGDPDALETI KASLKQFSKS FIAKAPHLRR
H
//