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Database: UniProt
Entry: A3VFU9_9RHOB
LinkDB: A3VFU9_9RHOB
Original site: A3VFU9_9RHOB 
ID   A3VFU9_9RHOB            Unreviewed;       572 AA.
AC   A3VFU9;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:EAQ12725.1};
DE            EC=2.2.1.6 {ECO:0000313|EMBL:EAQ12725.1};
GN   ORFNames=RB2654_06434 {ECO:0000313|EMBL:EAQ12725.1};
OS   Maritimibacter alkaliphilus HTCC2654.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Maritimibacter.
OX   NCBI_TaxID=314271 {ECO:0000313|EMBL:EAQ12725.1, ECO:0000313|Proteomes:UP000002931};
RN   [1] {ECO:0000313|EMBL:EAQ12725.1, ECO:0000313|Proteomes:UP000002931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2654 {ECO:0000313|EMBL:EAQ12725.1,
RC   ECO:0000313|Proteomes:UP000002931};
RX   PubMed=20729358; DOI=10.1128/JB.00873-10;
RA   Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA   Giovannoni S.J.;
RT   "Genome sequences of Pelagibaca bermudensis HTCC2601T and Maritimibacter
RT   alkaliphilus HTCC2654T, the type strains of two marine Roseobacter
RT   genera.";
RL   J. Bacteriol. 192:5552-5553(2010).
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:EAQ12725.1}.
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DR   EMBL; AAMT01000007; EAQ12725.1; -; Genomic_DNA.
DR   RefSeq; WP_008329863.1; NZ_VNHV01000005.1.
DR   AlphaFoldDB; A3VFU9; -.
DR   STRING; 314271.RB2654_06434; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_4_0_5; -.
DR   OrthoDB; 7534569at2; -.
DR   Proteomes; UP000002931; 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; cd02002; TPP_BFDC; 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:SF169; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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:UP000002931};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000313|EMBL:EAQ12725.1}.
FT   DOMAIN          12..142
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          214..343
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          419..563
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   572 AA;  60928 MW;  B298E77E1341F261 CRC64;
     MKGETPGDSP ITAGGAIFTK LKALGVSHVF TNAGTDFPPI IEGLVEAQRR GLDLPLPVTV
     PHEHAAVSMA HGFYQVSGRA QAVMLHTNVG LSNGATAIIN AWCDHIPMIV MSGRTPTTER
     GRFGARTVPI GWGQEMFDQE ALIREATKWQ YEIRFPEQVP ELLDRAWAIA NSGPKGPVYL
     SLPREVLCEP CPAEGISAPP RMTPVTTAPH GDAVARAARA LAQADNPVII AQRGAGGADG
     FAALTRFVED HAIPLVHYWP NQIAIPMGHP MQVGADPSPW LADADVVLAL DCLAPWMPDG
     VTLRDDATII QAAPDPLFGR TPVRNFPADI TLAGPVGATL AALIPAVGAE PRDETRIATR
     RAQVTAASET SRTAVIARAE AGASAPMTKD WVSLCLGRAL KGRRASVFHE LGCPLQPLDL
     DQPDSYFQEP FSGGLGWGMP AAIGAKMADP DRLVVATVGD GSYMFANPTA CHFVAEAQNV
     PVIVLVLNNE EWAAVRYSVQ GLYPEGESKT ANEVPLTSLR PSPDFAKVAE ASRAYTETVT
     DGRDLPAALE RAIRVAEKEQ RQVLLNIAIA RG
//
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