ID A0A2E7P034_9BURK Unreviewed; 570 AA.
AC A0A2E7P034;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:MBO15069.1};
GN ORFNames=CME87_06270 {ECO:0000313|EMBL:MBO15069.1};
OS Herbaspirillum sp.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1890675 {ECO:0000313|EMBL:MBO15069.1, ECO:0000313|Proteomes:UP000226028};
RN [1] {ECO:0000313|Proteomes:UP000226028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Graham E.D., Heidelberg J.F.;
RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT Global Oceans.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:MBO15069.1}.
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; PBPP01000043; MBO15069.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2E7P034; -.
DR Proteomes; UP000226028; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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:SF13; 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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 195..333
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 393..541
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 570 AA; 61346 MW; C1426DCFAC686D03 CRC64;
MTGADVLVKL LEEYGVEVIF GVPGDTNVAF YKALNRCGKV RHVMARDERS ALYMADAYAR
YSGKPGVAEC PSGAGAMYSL PGMAEANSSS IPLILLTNDI PLKGEGRGMI TELDNAKLFE
PVCKLSFQVK TTAKIPEAVR RAFRTATSGR PGAVHLTFPE DILAHASAST PDEIYAEPEC
RRFPAFPMRP DADLVRQLAA LLDASRRPVL VAGGGVMHSD GGAALLALAE KIDAAVVTTI
TGQGAVPDEH PLALGVIGDN GFHPHAARAV EESDLLVYLG CKMGSVVTIG WTFPSHQRER
QRVQVDIDPA VLGNTGRNDL NIAGDVRSVL QDLLPLVTQH EPRAWNAELN GMRRRFWEQA
QADLHSDALP LKPQRVVHEL NRRLPPRAVM VSDAGTPTPH MTRYLRLPGD GSRLVIPRAF
GGLGYAIPAV VGAWLARPDV RPIGLFGDGS FSMSCGELET LTRLQVPAVL LHFNNGCFGW
IKALQKLHND AQYLSVDFTR LDVARIAQGF GLKGLRAANA EELVAALDEA FASEGPVLID
IVSESIVDEC PPVYSWIKAM GKDPLAVGGA
//
