ID A3VMJ4_9RHOB Unreviewed; 475 AA.
AC A3VMJ4;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:EAQ10548.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:EAQ10548.1};
GN ORFNames=RB2654_00125 {ECO:0000313|EMBL:EAQ10548.1};
OS Maritimibacter alkaliphilus HTCC2654.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Maritimibacter.
OX NCBI_TaxID=314271 {ECO:0000313|EMBL:EAQ10548.1, ECO:0000313|Proteomes:UP000002931};
RN [1] {ECO:0000313|EMBL:EAQ10548.1, ECO:0000313|Proteomes:UP000002931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2654 {ECO:0000313|EMBL:EAQ10548.1,
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}.
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:EAQ10548.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAMT01000033; EAQ10548.1; -; Genomic_DNA.
DR AlphaFoldDB; A3VMJ4; -.
DR STRING; 314271.RB2654_00125; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_4_0_5; -.
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 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; 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 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 Transferase {ECO:0000313|EMBL:EAQ10548.1}.
FT DOMAIN 105..188
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 302..456
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 475 AA; 50537 MW; CBEEC62BE450E2C7 CRC64;
MLIYGATGPV DAALRRPWID WLHTCRDQAS MIRNYVKWDD QPGSMEAALE SMLRADVIAR
SEPKGPTYVN FDVSIQEKQH AQAPALPDFA RYQPPLPAAP SAEGVARAAD LLKNAKAPVV
LAGRVSRDPA DWARRVAFVE GLGAKVLTDI RIGASFPTDH PRHRGKPAFF IDDAAGAVLR
EADVILSLDW LDVAGTLKLA GEVTAQVIQA SLDYQLHNGW GMEHQALPAL DLHLACGPDV
AMHAIADALG VGAGEMPGDL PVKPALNAPD ADVELDIMTL AGALGEGLEG VCASFVRWPL
GWAGEAWHFR HPLDFLGSDG GAGIGSGPGM LIGAALALKD SDRLPVAVLG DGDFMMAASA
FWTAAHYGTP FLAVVSNNRS FYNDEVHQER VAVARNRPVE NKWIGQRIGD PDIDIAGVAR
AQGCEGIGPV FTAGELVEAI KQGVEMVRAG KSVVIDARVQ PGYNPNMVAG LTRSD
//