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
//