ID A0A061M0S2_9MICO Unreviewed; 548 AA.
AC A0A061M0S2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:EYT55938.1};
GN ORFNames=H490_0104840 {ECO:0000313|EMBL:EYT55938.1};
OS Leucobacter sp. UCD-THU.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1292023 {ECO:0000313|EMBL:EYT55938.1, ECO:0000313|Proteomes:UP000026917};
RN [1] {ECO:0000313|EMBL:EYT55938.1, ECO:0000313|Proteomes:UP000026917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-THU {ECO:0000313|EMBL:EYT55938.1,
RC ECO:0000313|Proteomes:UP000026917};
RX PubMed=23792744; DOI=10.1128/genomeA.00325-13;
RA Holland-Moritz H.E., Bevans D.R., Lang J.M., Darling A.E., Eisen J.A.,
RA Coil D.A.;
RT "Draft Genome Sequence of Leucobacter sp. Strain UCD-THU (Phylum
RT Actinobacteria).";
RL Genome Announc. 1:S69-S82(2013).
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:EYT55938.1}.
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DR EMBL; APJM01000007; EYT55938.1; -; Genomic_DNA.
DR RefSeq; WP_017883646.1; NZ_KB714601.1.
DR AlphaFoldDB; A0A061M0S2; -.
DR STRING; 1292023.H490_0104840; -.
DR HOGENOM; CLU_013748_3_1_11; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000026917; 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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF167; 2-KETOARGININE DECARBOXYLASE ARUI-RELATED; 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:UP000026917};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 12..123
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 200..331
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 398..540
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 548 AA; 57732 MW; D401DC0E5F391214 CRC64;
MLRSESPVDT VTLADAIARR LTQYGVEHVF GIPGTHNLEL FRSLGTAGIE VISAHHEQGL
GYAADAYSRV SSRPAVVVTT TGPGITNLIT ALATSLAASV PVLAIAPGIP EGGADGRAGW
LHDLPSQLGL MSRLVRSRRA QSGAAAVSFI DEVARSWQTE RPLPAYLEVP FDRFTAEEEL
ILGELPAFDT GSGWPAQAEI NRAAQRLVEA ERPVIVAGRG GANPEAAGSV RQIAEALGAP
VVTTANAKGV LDETHPLSLG VSLRVNAAKQ MLERSDAVLV VGSDLGSSEF WGPCPALGET
MIRVDVDAQM MHANARAPFP LLGRSELVMP RLAAAVAERR GAGSASNAWD AADLEAVAAD
LAAYGDGYRR FHEHVQDLTD PLDVAIAGDS SQVTYFGTAT YWKAQRPNRF LYPAGYGTLG
YAIPAAIGAV LTGEVDRVVA ITGEGGMLFS VQELATAAEL GLPVVTIVFT NGGYQEIRDG
MDSAGIAPVG VSFTAPDFVS LARGFRIEAR SVVADGMNEI GFREALEWAL AKNEPTLIEV
DVTGTMRR
//
