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Database: UniProt
Entry: C1F1H7_ACIC5
LinkDB: C1F1H7_ACIC5
Original site: C1F1H7_ACIC5 
ID   C1F1H7_ACIC5            Unreviewed;       576 AA.
AC   C1F1H7;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   SubName: Full=Acetolactate synthase, large subunit {ECO:0000313|EMBL:ACO34678.1};
DE            EC=2.2.1.6 {ECO:0000313|EMBL:ACO34678.1};
GN   Name=ivlB1 {ECO:0000313|EMBL:ACO34678.1};
GN   OrderedLocusNames=ACP_0577 {ECO:0000313|EMBL:ACO34678.1};
OS   Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM
OS   7670 / NBRC 15755 / NCIMB 13165 / 161).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Acidobacterium.
OX   NCBI_TaxID=240015 {ECO:0000313|EMBL:ACO34678.1, ECO:0000313|Proteomes:UP000002207};
RN   [1] {ECO:0000313|EMBL:ACO34678.1, ECO:0000313|Proteomes:UP000002207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 /
RC   NCIMB 13165 / 161 {ECO:0000313|Proteomes:UP000002207};
RX   PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP001472; ACO34678.1; -; Genomic_DNA.
DR   RefSeq; WP_015895763.1; NC_012483.1.
DR   AlphaFoldDB; C1F1H7; -.
DR   STRING; 240015.ACP_0577; -.
DR   KEGG; aca:ACP_0577; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_1_3_0; -.
DR   InParanoid; C1F1H7; -.
DR   OMA; QLQRESY; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000002207; 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   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:SF13; ACETOLACTATE SYNTHASE, CHLOROPLASTIC; 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:UP000002207};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000313|EMBL:ACO34678.1}.
FT   DOMAIN          1..124
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          197..330
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          393..543
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   576 AA;  61978 MW;  56D6CEE429FD2EB8 CRC64;
     MKASDYIASV LQQQRVAAVF ELVGGMITHM IDSVFVQGEV PIVSMHHEQG AAFAAEAVGK
     ITGIPGVAMA TSGPGATNLL TGVGSCYFDS SPAVFITGQV NRHEQKGNRA VRQLGFQETD
     IVSMARPVTK HSVLVQDVRD LPNTLHGAFR LATDKRPGPV LIDIPMDVQR ENVEPEWLMH
     HAADAPLLPE ERDLVALKEA LLKAQRPLVL AGGGVRAGRV TAEFRQMVEM LSIPVVHSLM
     GVDALPWSHT LNAGMIGSYG NRWSNLAISQ CDLLVVVGSR LDVRQTGADT QGFKEGRQIF
     HLDCDAGEMN NRVTGCHAIL GELRPALLAL HEMLLPIRDT VAANCMHWLG EIAALRRRWP
     DTQEIPDLQG INPNSFMHGL SQAGASAGAY VVDVGQHQMW AAQSLEIADD QRFLTSGGMG
     SMGFALPAGI GAAIALAGQP VVVIAGDGGF QCNIQELQTV ARLGLPIKIV VVNNNCLGMV
     RQFQESYFKG RYRSTLWGYT APDFEAVAKA YGIPSKSISD PTQIASASEW LFADHQSPAL
     LQVMVSPNAN AYPKLAFGKG MTSMEPQEKP IAMEGT
//
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