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Database: UniProt
Entry: A3VMJ4_9RHOB
LinkDB: A3VMJ4_9RHOB
Original site: A3VMJ4_9RHOB 
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}.
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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
//
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