ID W2EY97_9ACTN Unreviewed; 583 AA.
AC W2EY97;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:ETK36649.1};
GN ORFNames=MPTA5024_08215 {ECO:0000313|EMBL:ETK36649.1};
OS Microbispora sp. ATCC PTA-5024.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=316330 {ECO:0000313|EMBL:ETK36649.1, ECO:0000313|Proteomes:UP000018869};
RN [1] {ECO:0000313|EMBL:ETK36649.1, ECO:0000313|Proteomes:UP000018869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PTA-5024 {ECO:0000313|EMBL:ETK36649.1,
RC ECO:0000313|Proteomes:UP000018869};
RX PubMed=24459268;
RA Sosio M., Gallo G., Pozzi R., Serina S., Monciardini P., Bera A.,
RA Stegmann E., Weber T.;
RT "Draft Genome Sequence of the Microbispora sp. Strain ATCC-PTA-5024,
RT Producing the Lantibiotic NAI-107.";
RL Genome Announc. 2:e01198-13(2014).
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:ETK36649.1}.
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DR EMBL; AWEV01000071; ETK36649.1; -; Genomic_DNA.
DR RefSeq; WP_036321147.1; NZ_KI866522.1.
DR AlphaFoldDB; W2EY97; -.
DR STRING; 316330.MPTA5024_08215; -.
DR PATRIC; fig|316330.3.peg.1589; -.
DR HOGENOM; CLU_013748_3_4_11; -.
DR OrthoDB; 3203527at2; -.
DR Proteomes; UP000018869; 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: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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000018869};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..105
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 218..348
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 424..564
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 192..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 583 AA; 60355 MW; A7F1F27969C29EA7 CRC64;
MNVAEAVGAV LASLGVRAAF GVVGSGNFHV TNALVAGGVR YVAARHEGGA ATMADAYARM
SGTVAVLTVH QGPGLTNALT GITEAAKSRT PLLVLAPEAA SARSNFALDQ AALAAAVGAH
GARVGSAETV VDDTVMAYLA ALLGRRTVVL TLPLDVQAEE LPEEAVHAVR DLRAGPGGAH
REAASRIAGP WGLTFPAERD TSGGDPEDLP EEPSDAMTRL AGLLARAERP VFVAGRGARG
ARRELEALGE RVGALFATSA VAKGHFHGSP WDLDVIGGFA SPLAAELVRG ADLVVGWGCS
FTMWTTRHGA LIGPDATVVQ VDLDPDALGV NRPVDLGVIG DVRETARAVG ALVDGLAPAG
DPSSRGYRSP GLAERIAREV RWRDVPYEDA TGGGRIDPRT LTIGLDDLLP AERVVAVDSG
NFMGYPSMFL AVPDGSAFCF TQAFQAIGLG LATAIGAALA QPDRLPVAAL GDGGALMSVA
ELETVVRLGL PMVVVVYDDE AYGAEVHHFG PHGFPLETVT FPPVDIAEIA RGFGCAAVTV
RDERDLGGVA EWLKGPRDRP LVVHAKVTGD APSWWLEEAF RGH
//
