ID G9ZPW4_9LACO Unreviewed; 558 AA.
AC G9ZPW4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:EHL98027.1};
GN ORFNames=HMPREF9103_01769 {ECO:0000313|EMBL:EHL98027.1};
OS Lentilactobacillus parafarraginis F0439.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=797515 {ECO:0000313|EMBL:EHL98027.1, ECO:0000313|Proteomes:UP000004625};
RN [1] {ECO:0000313|EMBL:EHL98027.1, ECO:0000313|Proteomes:UP000004625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0439 {ECO:0000313|EMBL:EHL98027.1,
RC ECO:0000313|Proteomes:UP000004625};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) 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:EHL98027.1}.
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DR EMBL; AGEY01000089; EHL98027.1; -; Genomic_DNA.
DR RefSeq; WP_008213116.1; NZ_JH414975.1.
DR AlphaFoldDB; G9ZPW4; -.
DR STRING; 797515.HMPREF9103_01769; -.
DR PATRIC; fig|797515.3.peg.1633; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_2_9; -.
DR Proteomes; UP000004625; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:InterPro.
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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..330
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 558 AA; 60901 MW; E64E785507439D35 CRC64;
MADKKRGSQA LIKSMINQDI KYVFGIPGAK VDQLFEDLQY SDQPNAPQLI VTRHEQNAAF
IAQGIGRLTG KPGVVATTSG PGVSNLVTGL MTATAEGDPV IGLGGQVPRD DLARLTHQSI
PSKELMSVAA KSSVEVQDAN NLSEAFTNAY NTATSGKAGA TFISLPSDVL SDNVERPEMA
PLAKSERTQT SPTTLNKVID MIKNAKLPVI LAGMRASSQE VTESLHKLLE KVALPVVETY
QGAGVISHEL IDDYFGRVGL FRNQIGDTLL KQSDLVIAVG YDPVEYEARN WNVEHNDQII
NIDSISPELT VDYQPDVVIE ADIAGTLDAL TDALPADYKL STETVHQLTE LRQVFDRQNE
VKTTAKPGTI HPIDIVNELQ KKVDDNTTVT VDVGSHYIWM ARHFRIYRPR HLLFSNGMQT
LGVSLPWAIA AKLVRPNEKV VSVSGDGGFL FSGQELETAV RLNLNIVQLI WDDGYYDMVK
FQEEAKYGKN AGVKLGKVNF VKYAESFGAT GLRATNPDEL SQALDQAFNA NGPVIIDIPV
DYSDNIKLKS ALLKDILN
//
