ID A0A1E7JS86_9ACTN Unreviewed; 566 AA.
AC A0A1E7JS86;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:OEU91762.1};
GN ORFNames=AN215_04485 {ECO:0000313|EMBL:OEU91762.1};
OS Streptomyces abyssalis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=933944 {ECO:0000313|EMBL:OEU91762.1, ECO:0000313|Proteomes:UP000176087};
RN [1] {ECO:0000313|EMBL:OEU91762.1, ECO:0000313|Proteomes:UP000176087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 10390 {ECO:0000313|EMBL:OEU91762.1,
RC ECO:0000313|Proteomes:UP000176087};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(2016).
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:OEU91762.1}.
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DR EMBL; LJGT01000037; OEU91762.1; -; Genomic_DNA.
DR RefSeq; WP_070010113.1; NZ_LJGT01000037.1.
DR AlphaFoldDB; A0A1E7JS86; -.
DR STRING; 933944.AN215_04485; -.
DR PATRIC; fig|933944.5.peg.1768; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000176087; 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:UP000176087};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 16..125
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 206..332
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 399..548
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 566 AA; 60996 MW; B52C9B1996CEC82E CRC64;
MPDDSQDSRD NQDLISGGHL VAKALKAEGV EVIYTLCGGH IIDIYDGCVD EGIDVVDVRH
EQVAAHAADG YARLTGKPGC AVVTAGPGTT DAVTGVANAF RAESPMLLIG GQGAHTQHKM
GSLQDLPHVD MMTPITKFAS TVPDTARAAD MVSMAFRECY HGAPGPSFLE IPRDVLDAKV
PVEKARVPKT GNYRASTRQP GDPEDVQKLA DLLVQAERPA ILLGSQTWTC RATDAATELV
RTLNVPAYMN GAGRGTLPPG DPHHFQLSRR YAFSNADLII IVGTPFDFRM GYGKRLSQDA
TVVQIDLDYR TVGKNRDIDL GIVGSADLVL SAVTQAASGR LNGGGDKRKA WLEELRSAEQ
TALDKRLPQL RSDASPIHPY RLVSEINDFL TEDSLYIGDG GDIVTFSGQV VQPKAPGNWM
DPGPLGTLGV GVPFVLAAKQ ARPDKEVVAL FGDGAFSLTG WDFETLVRYN LPFVGIVGNN
SSMNQIRYGQ KAKYGEERER VGNTLGDVPY EEFARMLGGH GEVVREPSEI RPALDRARAS
GKPSLVNVWI DPDAYAPGTM NQTMYK
//
