ID S3ZCV0_9ACTN Unreviewed; 564 AA.
AC S3ZCV0;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Putative acetolactate synthase {ECO:0000313|EMBL:EPH40963.1};
GN ORFNames=STRAU_5959 {ECO:0000313|EMBL:EPH40963.1};
OS Streptomyces aurantiacus JA 4570.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=1286094 {ECO:0000313|EMBL:EPH40963.1, ECO:0000313|Proteomes:UP000014629};
RN [1] {ECO:0000313|EMBL:EPH40963.1, ECO:0000313|Proteomes:UP000014629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA 4570 {ECO:0000313|EMBL:EPH40963.1,
RC ECO:0000313|Proteomes:UP000014629};
RA Gruening B.A., Praeg A., Erxleben A., Guenther S., Mueller M.;
RT "Draft Genome Sequence of Streptomyces aurantiacus, Which Produces
RT Setomimycin.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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:EPH40963.1}.
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DR EMBL; AOPZ01000355; EPH40963.1; -; Genomic_DNA.
DR RefSeq; WP_016644080.1; NZ_AOPZ01000355.1.
DR AlphaFoldDB; S3ZCV0; -.
DR PATRIC; fig|1286094.4.peg.5892; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000014629; 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; cd02004; TPP_BZL_OCoD_HPCL; 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:SF166; 2-HYDROXYACYL-COA LYASE 2; 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:UP000014629};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 14..123
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 204..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 397..546
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 564 AA; 60371 MW; CFA3395C8885C81F CRC64;
MPDDSSSDNN TLISGGHLVA KALKAEGVEV IYTLCGGHII DIYDGCVDEG IDVVDVRHEQ
VAAHAADGYA RITGKPGCAV VTAGPGTTDA VTGVANAFRA ESPMLLIGGQ GAHTQHKMGS
LQDLPHVDMM TPITKFAATV PDTARAADMV SMAFRECYHG APGPSFLEIP RDVLDAKVPA
DKARVPRAGH YRASTRSAGD PEAIEKLADL LVHAEKPAIL LGSQVWTTRG TAEAIELVRA
LNVPAYMNGA GRGTLPPGDP HHFQLSRRYA FSNADLIVIV GTPFDFRMGY GKRLSPEATV
VQIDLDYRTV GKNRDIDLGI VGDAGLVLKS VTAAASGRVN GGASRRKEWL DELRAAEQTA
LEKRLPSLKS DASPIHPYRL VSEINDFLTE DSIYIGDGGD IVTFSGQVVQ PKAPGHWMDP
GPLGTLGVGV PFVLAAKQAR PDKEVVALFG DGAFSLTGWD FETLVRYNLP FVGIVGNNSS
MNQIRYGQKA KYGTERERVG NTLGDVHYDK FAQMLGGHGE EVRDPADIGP ALRRARESGK
PSLINVWVDP DAYAPGTMNQ TMYK
//
