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Database: UniProt
Entry: G5IB94_9CLOT
LinkDB: G5IB94_9CLOT
Original site: G5IB94_9CLOT 
ID   G5IB94_9CLOT            Unreviewed;       624 AA.
AC   G5IB94;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF9473_00816 {ECO:0000313|EMBL:EHI61201.1};
OS   Hungatella hathewayi WAL-18680.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX   NCBI_TaxID=742737 {ECO:0000313|EMBL:EHI61201.1, ECO:0000313|Proteomes:UP000005384};
RN   [1] {ECO:0000313|EMBL:EHI61201.1, ECO:0000313|Proteomes:UP000005384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAL-18680 {ECO:0000313|EMBL:EHI61201.1,
RC   ECO:0000313|Proteomes:UP000005384};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., Summanen P.H.,
RA   Molitoris D.R., Song M., Daigneault M., Allen-Vercoe E., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Clostridium hathewayi WAL-18680.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHI61201.1}.
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DR   EMBL; ADLN01000006; EHI61201.1; -; Genomic_DNA.
DR   RefSeq; WP_006778802.1; NZ_JH379027.1.
DR   AlphaFoldDB; G5IB94; -.
DR   PATRIC; fig|742737.3.peg.811; -.
DR   HOGENOM; CLU_013748_1_3_9; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000005384; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd00568; TPP_enzymes; 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; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF142; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005384};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          3..116
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          210..345
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          425..575
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   624 AA;  67928 MW;  DA99EFAE590EEC3D CRC64;
     MKMKVSNYIA EQLVAHGLSQ VFTVTGGGAM HLNDALGHEE GLHCLYQHHE QACAMAAESY
     ARIHNQPAVL CVTTGPGGTN AITGVVGGWL DSIPMLVLSG QVRYDTTARW SGVGIRAMGD
     QEFDIVKAIG CMTKYSEMVT DPMRIRYCLE KAIYLATSGR PGPAWLDIPL DVQGAFIEME
     ELEGFDSAAF EAGEESQGLP APVTEETARA IIEKIRGAKR PVINAGNGIR IAGAYPVFAR
     VVKMLGVPVA TGWNSQDCMC SEDELYVGRA GNMGDRPGNF AIQNSDLVFS VGSRLSIRQV
     GYNYKTWARA AYTIVNDIDI EELKKPSVHV DMMVHADARD LLEALERVLL QEQKADGDAL
     PAFKGGEGLP GMSWLETCQM WKKKYPVVLP RHMEVGDDKP ANVYALVQEL SSRLEEGQIT
     VVGNGSACVA GGHGWIIKPG QRFISNSAIA SMGYDLPAAI GACMADSSQD IVLLTGDGSI
     QMNIQELQTI IHHRMPIKIF LINNGGYHSI RQTQKNYFGE PLVGIGVDSH DLSFPDMEKL
     AGAYGYPYVR ACHNSELAEA VEMTLAMDGP VICEVLVSME QNFEPKSAAK RLPDGTMVSP
     PLEDLSPFLP EEEMDMNMII PRIK
//
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