GenomeNet

Database: UniProt
Entry: D7H964_VIBCL
LinkDB: D7H964_VIBCL
Original site: D7H964_VIBCL 
ID   D7H964_VIBCL            Unreviewed;       567 AA.
AC   D7H964;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:EFH75595.1};
GN   ORFNames=VCRC385_01149 {ECO:0000313|EMBL:EFH75595.1};
OS   Vibrio cholerae RC385.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345074 {ECO:0000313|EMBL:EFH75595.1, ECO:0000313|Proteomes:UP000004696};
RN   [1] {ECO:0000313|Proteomes:UP000004696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RC385 {ECO:0000313|Proteomes:UP000004696};
RA   Heidelberg J.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EFH75595.1, ECO:0000313|Proteomes:UP000004696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RC385 {ECO:0000313|EMBL:EFH75595.1,
RC   ECO:0000313|Proteomes:UP000004696};
RG   The Broad Institute Genome Sequencing Platform;
RA   Colwell R., Grim C.J., Young S., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R., Heiman D.,
RA   Hepburn T., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA   Pearson M., Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Walk T., White J., Yandava C., Borodovsky M.,
RA   Heidelberg J., Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Vibrio cholerae RC385.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GG774555; EFH75595.1; -; Genomic_DNA.
DR   RefSeq; WP_001191535.1; NZ_GG774555.1.
DR   AlphaFoldDB; D7H964; -.
DR   GeneID; 66939446; -.
DR   PATRIC; fig|345074.23.peg.3539; -.
DR   HOGENOM; CLU_013748_3_2_6; -.
DR   Proteomes; UP000004696; Unassembled WGS sequence.
DR   GO; GO:0003984; F:acetolactate synthase activity; 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:0034077; P:butanediol metabolic process; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          9..123
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          390..535
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   567 AA;  61925 MW;  EA28D2B036896F4E CRC64;
     MQSNIHLRSG AQLIAQQLEA IGVRYVFGIP GAKIDRLFDA IEDTKIQMIP VRHEANGAFM
     AGIMGRLSGR AGVTLATSGP GCGNLVTGVA TANSEGDPMI AIGGAVKRDY QQKQTHQSMD
     TVSIFRSITK YSAEIQHVDA TSEIMANAFR LAESGRQGAC FISVPQDVLA DKTSSEIIIP
     SAYQPTAEAD PDSLQEAVER IQKAQRCVVL LGLHASHQAT AEAVSAFLHK TQLPVVGTYQ
     AAGAVDINYY HHFAGRVGLF NNQPGDVLLK EADLIITIGF NPIEYDPELW NSQRCPIVHI
     DIEPAQYQIH YQPCLQIVGN IASNLAALCR PLPGFTRLSP TALAILEEVT QQRHAIKAYP
     LRYQNAGFHP LTLIKTMQAI IKPDTTLCLD MGSFHIWIAR YLSCFRARQM LVSNGQQTMG
     VALPWAIAAS LLKPGHKVVS VSGDGGFMQS SMELETAVRL KCNIVHIIWV DNAYNMVEMQ
     EVQKYHRAAG VKFGPIDFKA YAESFGARGY AITQPDQLLP TLRQAMEVEG PAVVAIPVDY
     SDNPKLMQAR TEANQDPVFQ TLEGVFA
//
DBGET integrated database retrieval system