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Database: UniProt
Entry: Q4FPQ4_PELUB
LinkDB: Q4FPQ4_PELUB
Original site: Q4FPQ4_PELUB 
ID   Q4FPQ4_PELUB            Unreviewed;       588 AA.
AC   Q4FPQ4;
DT   30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2005, sequence version 1.
DT   20-DEC-2017, entry version 84.
DE   RecName: Full=Acetolactate synthase {ECO:0000256|RuleBase:RU003591};
DE            EC=2.2.1.6 {ECO:0000256|RuleBase:RU003591};
GN   Name=ilvB {ECO:0000313|EMBL:AAZ20828.1};
GN   OrderedLocusNames=SAR11_0003 {ECO:0000313|EMBL:AAZ20828.1};
OS   Pelagibacter ubique (strain HTCC1062).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Pelagibacterales;
OC   Pelagibacteraceae; Candidatus Pelagibacter.
OX   NCBI_TaxID=335992 {ECO:0000313|EMBL:AAZ20828.1, ECO:0000313|Proteomes:UP000002528};
RN   [1] {ECO:0000313|EMBL:AAZ20828.1, ECO:0000313|Proteomes:UP000002528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC1062 {ECO:0000313|EMBL:AAZ20828.1,
RC   ECO:0000313|Proteomes:UP000002528};
RX   PubMed=16109880; DOI=10.1126/science.1114057;
RA   Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L.,
RA   Baptista D., Bibbs L., Eads J., Richardson T.H., Noordewier M.,
RA   Rappe M.S., Short J.M., Carrington J.C., Mathur E.J.;
RT   "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL   Science 309:1242-1245(2005).
CC   -!- CATALYTIC ACTIVITY: 2 pyruvate = 2-acetolactate + CO(2).
CC       {ECO:0000256|RuleBase:RU003591}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU003591};
CC       Note=Binds 1 Mg(2+) ion per subunit.
CC       {ECO:0000256|RuleBase:RU003591};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|RuleBase:RU003591};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000256|RuleBase:RU003591};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 1/4.
CC       {ECO:0000256|RuleBase:RU003591}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC       from pyruvate: step 1/4. {ECO:0000256|RuleBase:RU003591}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|RuleBase:RU003591}.
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DR   EMBL; CP000084; AAZ20828.1; -; Genomic_DNA.
DR   RefSeq; WP_011281400.1; NC_007205.1.
DR   ProteinModelPortal; Q4FPQ4; -.
DR   STRING; 335992.SAR11_0003; -.
DR   EnsemblBacteria; AAZ20828; AAZ20828; SAR11_0003.
DR   KEGG; pub:SAR11_0003; -.
DR   eggNOG; ENOG4105C7K; Bacteria.
DR   eggNOG; COG0028; LUCA.
DR   HOGENOM; HOG000258448; -.
DR   KO; K01652; -.
DR   OMA; MRSYNPV; -.
DR   OrthoDB; POG091H02KO; -.
DR   UniPathway; UPA00047; UER00055.
DR   UniPathway; UPA00049; UER00059.
DR   Proteomes; UP000002528; Chromosome.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1220; -; 1.
DR   InterPro; IPR012846; Acetolactate_synth_lsu.
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; IPR011766; TPP_enzyme-bd_C.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00118; acolac_lg; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003591};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|RuleBase:RU003591};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002528};
KW   Magnesium {ECO:0000256|RuleBase:RU003591};
KW   Metal-binding {ECO:0000256|RuleBase:RU003591};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002528};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU003591};
KW   Transferase {ECO:0000256|RuleBase:RU003591,
KW   ECO:0000313|EMBL:AAZ20828.1}.
FT   DOMAIN        7    171       TPP_enzyme_N. {ECO:0000259|Pfam:PF02776}.
FT   DOMAIN      195    330       TPP_enzyme_M. {ECO:0000259|Pfam:PF00205}.
FT   DOMAIN      400    547       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   588 AA;  65246 MW;  254FDC7A18E714C6 CRC64;
     MPKLYSGAEI VFKCLEDQKV EHIFGYPGGA VLPIYDELKN HPTIKHILVR HEQGAGHAAE
     GYARSTGKPG VVLVTSGPGA TNVVTALTDA YMDSVPLVCI SGQVPTHLIG TDAFQECDTT
     GITRPCTKHN WLVKDINDLP RIMHEAFEVA TTGRPGPVLV DIPKDIQFAK TKYSKPNKDK
     KVVTKNLNRF NQKNIDQLIE LMSKSKKPIF YTGGGVINSG PKASELLREL VSLTGFPITS
     TLQGLGAYPG NDNQFLGMLG MHGTYEANNA MHDCDLLINI GARFDDRITG KIDEFSPKSK
     KVHIDIDPSS INKIVKVDLS IVGDVSDVIS STTKTLKKKK LNLEKSNKQK ISNWWLQIEK
     WRTKQSLSFV NSDTIIKPQY AVQRLYELTK NSDTYITTEV GQHQMWAAQH YKFDKPNRWM
     TSGGLGTMGY GLPAAIGVQV AHPKKLVVDI AGEASILMNM QEISTAVQYN LPIKIFILNN
     QYMGMVRQWQ ELLHEKNYSE SYSKALPDFV KLAEAYGCVG IRAKDPSELD EKIEEMINTD
     RPVIFDCLVD QGENCFPMIP SGKPHNQMLL GPKDQDANKI TGKGKALV
//
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