ID A0A1G9K7H4_9ACTN Unreviewed; 548 AA.
AC A0A1G9K7H4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SDL45619.1};
GN ORFNames=SAMN05421869_12629 {ECO:0000313|EMBL:SDL45619.1};
OS Nonomuraea jiangxiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=633440 {ECO:0000313|EMBL:SDL45619.1, ECO:0000313|Proteomes:UP000199202};
RN [1] {ECO:0000313|EMBL:SDL45619.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6533 {ECO:0000313|EMBL:SDL45619.1};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNDJ01000026; SDL45619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9K7H4; -.
DR STRING; 633440.SAMN05421869_12629; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000199202; 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:UP000199202};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..317
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 386..533
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 548 AA; 57763 MW; 04891BA260122AFB CRC64;
MESAKHAGDA AVTVSKAYGV ETMFTLSGGH VFPLYDGAVH EGMRILDVRH EQSAVFAAEA
TARLTRKPGL AVLTAGPGIT NGVSGVATAH FNGSPVVVMG GRAPQSRWGS GALQELDHPP
LLEPITKLAF TATGAESIGQ DVEMAFRTAI APHRGPVFLD FYMDHLFAPS PSHDVHSQTP
SPLEPDPEAL AGIARLLAEA ERPVLVYGSD VWMDRAEEAA RDFAETWRLP VIPNGQGRGI
LPSGHELLVT RARGLALSQA DLVIVVGTPL DFRLNYGWFG GKEGAPLARV VHIADAPSQL
ATHMQPAASA AGDLSVVFWG LGAACGEAGV KPDRYGTWVS KLHETAAAAI AGDAELLAAD
SDPIHPMRIY GELGKLLADD AVVIGDGGDF VSYAGKYVEP KQPGNWLDPG PYGCLGTGLG
YSVAARLARP SSQVVLLLGD GAAGFSLMDV DTLVRHRLPV VMICGNNGIW GLEKHPMQLL
YGYDVAAELQ PQCRYDQVVT ALGGGGELVT KPSEIGPALR RAFDSGIPYM VNIATDPQIA
YPRNTTGV
//
