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Database: UniProt
Entry: Q0FGP6_9RHOB
LinkDB: Q0FGP6_9RHOB
Original site: Q0FGP6_9RHOB 
ID   Q0FGP6_9RHOB            Unreviewed;       545 AA.
AC   Q0FGP6;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   SubName: Full=Acetolactate synthase II large subunit {ECO:0000313|EMBL:EAU52593.1};
DE            EC=2.2.1.6 {ECO:0000313|EMBL:EAU52593.1};
GN   ORFNames=OM2255_03675 {ECO:0000313|EMBL:EAU52593.1};
OS   Rhodobacterales bacterium HTCC2255.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales.
OX   NCBI_TaxID=367336 {ECO:0000313|EMBL:EAU52593.1, ECO:0000313|Proteomes:UP000009381};
RN   [1] {ECO:0000313|EMBL:EAU52593.1, ECO:0000313|Proteomes:UP000009381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2255 {ECO:0000313|EMBL:EAU52593.1,
RC   ECO:0000313|Proteomes:UP000009381};
RA   Giovannoni S., Cho J.-C., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA   Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (SEP-2006) 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:EAU52593.1}.
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DR   EMBL; AATR01000001; EAU52593.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0FGP6; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_4_5; -.
DR   OrthoDB; 4494979at2; -.
DR   BioCyc; RBAC367336:G1GNW-180-MONOMER; -.
DR   Proteomes; UP000009381; Unassembled WGS sequence.
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:0044281; P:small molecule metabolic process; IEA:UniProt.
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:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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:UP000009381};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000313|EMBL:EAU52593.1}.
FT   DOMAIN          5..121
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          196..329
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          384..529
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   545 AA;  60123 MW;  9C2EE239D4158135 CRC64;
     MTQKRAANLL VECLINQGVD KIYGVPGESY LSVLDALYDF NDKINFISTR HESAASFMAE
     AYGKLTGEVG ICFVTRGPGA TNASIGVHTA MQNSSPMILF IGQIGRDMTE REAFQEIDYK
     AYFGSISKWV VQVNNADRLP EIIGRAFSMA LSGRPGPVVV SLPEDMLRDL TSAVAINKIQ
     KTCAEISVTQ VNLIKDELEN SKKPLIICGG GGWSDIGRDY LKRFAESVNI PVICGFRNQD
     LMDTNSFAYV GDASFGKPQY IKDLIKNSDL ILAINIRFGE VITDAWSLFE FPHPKQKIIH
     THVSEAEINK VYHCEFGVVA NPDSVMQGLH EASVSKKPSD ALRRNKEDFV KSRKMVDAHG
     TLNVAKICNY LNIHSDKDAI FTNGAGNFAI WSGKYLNYSK EHRLLAPQAG AMGAGVPAAL
     AAKSIFPNRQ VICFAGDGDF QMSSSELGTA MQEGLNPIIL IHNNGSYGTI RMHQEMRYPK
     RVSGTNLKNP NFKCIAEAYN FGYSKITNLS EFRVAFEKAK TFDVCFIIEM LADIKDISPG
     KIIDL
//
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