ID A0A252B6H1_9PROT Unreviewed; 562 AA.
AC A0A252B6H1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:OUI99972.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:OUI99972.1};
GN ORFNames=HK20_00530 {ECO:0000313|EMBL:OUI99972.1};
OS Acetobacter sp. DsW_54.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=1670660 {ECO:0000313|EMBL:OUI99972.1, ECO:0000313|Proteomes:UP000194822};
RN [1] {ECO:0000313|EMBL:OUI99972.1, ECO:0000313|Proteomes:UP000194822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DsW_54 {ECO:0000313|EMBL:OUI99972.1};
RA Ju J., Zhang J.;
RL Submitted (JUN-2014) 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:OUI99972.1}.
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DR EMBL; JOPD01000005; OUI99972.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A252B6H1; -.
DR Proteomes; UP000194822; 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 GO; GO:0034077; P:butanediol metabolic process; IEA:InterPro.
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; IPR012782; Acetolactate_synth_catblc.
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 NCBIfam; TIGR02418; acolac_catab; 1.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000194822};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:OUI99972.1}.
FT DOMAIN 12..125
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..331
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 392..538
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 562 AA; 59651 MW; 2D383658922C51FE CRC64;
MTKMADTTAQ CGAELIVKNL EAHGITHVFG IPGAKVDRLF DALVDSSIET VVTRHEQNAA
FIAGGLGRIT GKAGVCIATS GPGASNFITG LATANSEGDP VLAIGGAVKL ADRLKLTHQT
MDTVSLFRPV TKYSVELTTP TAISEVMANA FRFAESGRPG AAFVSTPMDV LSMPANAPVL
ADRLAPRMGG APADVVAEAA TLLKKARRPV MLLGMLASRP DVADAVRAFV KQTGVPVVGT
YQAAGAVSEE LVDRFGGRIG LFRNQHGDQL LHEADVVVAV GYNPVEYDPW LWNVNDARQI
INVDIVAAEL DNAFVPAIEL IGDIALTLEG LGGKAGGLAR APELEAVLEG YKKARSTALL
TARSSSNSAV HPLQIVRELE QFVTPDMTLC LDMGTFHIWL ARYLLSFRAR QVLISNGQQT
MGVGLPWGIA ASLVNPSQKV VSISGDGGFM MSSMELETAV RLKCNLIHMV WIDQAYNMVE
IQEQKKYGRG SGVHFGPIDF AKYAEACGAK GITATTEDGV RQALREAMDV EGPVVIAVPV
DYSHNHLLMQ PLAQLGETTA AA
//
