ID A0A177HZ31_9ACTN Unreviewed; 558 AA.
AC A0A177HZ31;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:OAH15960.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:OAH15960.1};
GN Name=alsS {ECO:0000313|EMBL:OAH15960.1};
GN ORFNames=STSP_06630 {ECO:0000313|EMBL:OAH15960.1};
OS Streptomyces jeddahensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH15960.1, ECO:0000313|Proteomes:UP000077381};
RN [1] {ECO:0000313|EMBL:OAH15960.1, ECO:0000313|Proteomes:UP000077381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381};
RA Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J., Madkour M.H.,
RA Al-Ansari A.M., Almakishah N.H., Steinbuechel A., Daniel R.;
RT "Genome sequence of Streptomyces sp. G25.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:OAH15960.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LOHS01000029; OAH15960.1; -; Genomic_DNA.
DR RefSeq; WP_067271705.1; NZ_LOHS01000029.1.
DR AlphaFoldDB; A0A177HZ31; -.
DR STRING; 1716141.STSP_06630; -.
DR PATRIC; fig|1716141.3.peg.702; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000077381; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02010; TPP_ALS; 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:SF129; ACETOLACTATE SYNTHASE; 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:UP000077381};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:OAH15960.1}.
FT DOMAIN 14..126
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 200..334
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 391..536
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 558 AA; 59746 MW; F85FA0D935013878 CRC64;
MTGPSEFSDR DQHSAAELLV RCLENEGVRV VFGLPGEENL HLTFALARSG IRYILTRHEQ
AASFMAEMYG RVTGRAGVVS ATLGPGAINL QLGVADAMTN STPLVALSAQ VGHNRNYKET
HQFVDLVNMF APITKWSASV PSASAIPEML RRAFKTAETE RPGAVYLAVP EDVDAAPAAA
ELQPLPRYVV RAEAPSPAQI ARAAALLHNA RHPIVLAGHG AARNAAATSL TAFAGSLGLP
VATTFHGKGV IADDLINSMG SIGFMRRDYT NFGFDAADLI IAVGYELQEF DPARINPQRD
KKIIHVHRFP AEVDAHYSID LGIIGDISQS LDALSAAVSD RFRGPAPARC REMVQAELDR
GCADGRYPLA PQRIVADTRT ALGRDDVVLV DTGALKMWMA RLYPTYAPNT CLISNGLSAM
GFALPGALAV ALAEPDVKVL AAVGDGSFLM HSQEIETAVR EAIPLTVLIW EDNGYGLIEW
KMDLTLGEHD ATAFGNPDIV RYAESFGATG YRIAAAEELL PTLRTALDDP GVSIIACPVD
YSENLRLTAR LGQLDAAL
//