GenomeNet

Database: UniProt
Entry: A3U1C8_PSEBH
LinkDB: A3U1C8_PSEBH
Original site: A3U1C8_PSEBH 
ID   A3U1C8_PSEBH            Unreviewed;       572 AA.
AC   A3U1C8;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:EAQ02111.1};
GN   ORFNames=OB2597_20841 {ECO:0000313|EMBL:EAQ02111.1};
OS   Pseudooceanicola batsensis (strain ATCC BAA-863 / DSM 15984 / KCTC 12145 /
OS   HTCC2597) (Oceanicola batsensis).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudooceanicola.
OX   NCBI_TaxID=252305 {ECO:0000313|EMBL:EAQ02111.1, ECO:0000313|Proteomes:UP000004318};
RN   [1] {ECO:0000313|EMBL:EAQ02111.1, ECO:0000313|Proteomes:UP000004318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-863 / DSM 15984 / KCTC 12145 / HTCC2597
RC   {ECO:0000313|Proteomes:UP000004318};
RX   PubMed=20418400; DOI=10.1128/JB.00412-10;
RA   Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT   "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT   batsensis HTCC2597(TDelta).";
RL   J. Bacteriol. 192:3549-3550(2010).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:EAQ02111.1}.
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; AAMO01000009; EAQ02111.1; -; Genomic_DNA.
DR   RefSeq; WP_009804109.1; NZ_AAMO01000009.1.
DR   AlphaFoldDB; A3U1C8; -.
DR   STRING; 252305.OB2597_20841; -.
DR   HOGENOM; CLU_013748_3_1_5; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000004318; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; IPR000399; TPP-bd_CS.
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.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000004318};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          14..117
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          214..349
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          405..550
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   572 AA;  60006 MW;  B04ADED4A4688AD8 CRC64;
     MTIDPRYGSE IDAPDAIVDC LVEAGVRYVF GLSGGHTGRI FGALEKRQDD IRTILVREES
     LGAVMAETVG RISGRPGVLL GQGPWVLGNG LLGTIEAHLA SSPLLLLTDF SDTPGASLHA
     PYQSGTGGYG NWDARGAFGA VTKEVFTAED PKTAVIATQL ALKHAMLGEP GPVAMIYGLQ
     ALAGSIDPAA RPRIFPTRAH VRPLAPATPD LSGVLERLAT AERPVILAGN GVRVGDAEAA
     LAGLVETTGL PVVTSPAGKG VFDDDHPLSR GVYGSYGNPS ANRAIHRADV ILALGTKLSA
     SDTVAGDPDL IDPARQSLIQ VDIEPRNLSW TLPVDLPVLG DLRPVLEALA AAWNTGPVAD
     WSGADNTPRM APLPASAPGA TAIFPQEIVA AMQRVLPEDT IYTCDAGENR IFMLHCLRPR
     GAGRFIQPAG AGPMGYALPS ALARKLMAPD SPIVAFSGDG GFSMTMNGLL SAVEAGLPII
     SVVMNNDALG WSQHSRNAFA TQFGRVDYAA IGRGMGCGGM KVSGLTELED ALKEALRVTR
     EDARPMVIDV ETSMDLSFAR LSYTETRALW MN
//
DBGET integrated database retrieval system