ID A0A316DVC3_9BACT Unreviewed; 575 AA.
AC A0A316DVC3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:PWK21408.1};
GN ORFNames=LV89_03701 {ECO:0000313|EMBL:PWK21408.1};
OS Arcicella aurantiaca.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Arcicella.
OX NCBI_TaxID=591202 {ECO:0000313|EMBL:PWK21408.1, ECO:0000313|Proteomes:UP000245489};
RN [1] {ECO:0000313|EMBL:PWK21408.1, ECO:0000313|Proteomes:UP000245489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22214 {ECO:0000313|EMBL:PWK21408.1,
RC ECO:0000313|Proteomes:UP000245489};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAY-2018) 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:PWK21408.1}.
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DR EMBL; QGGO01000024; PWK21408.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316DVC3; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000245489; 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; 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:SF142; 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:UP000245489};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..124
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 202..330
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..532
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 575 AA; 64211 MW; 9C073ABCF94B5D66 CRC64;
MKASDYIAKF IELKGIGYVF ELSGGMITHL LDSLNQVTSI KVVTMHHEQS ASFAADAYGR
VTGLPGVALA TSGPGATNLL TGIASCYFDS SPAIFITGQV NLHEQKGNRS IRQLGFQETD
IVSMAEPITK KCFRVENVND IPQILNEAFR ISTEGRPGPI LIDIPMNIQR ENIPLAEIIF
DCEDKNLNYN LELSKLNELS VSISTSKKPL LLIGRGIKSS FSDDELKIFL QLTKIPVVTT
LLAIDSLDSV NEQKIGFIGS YGNRWANIAF GECDLLIVLG SRLDIRQTGA DTKFFEDRII
YHIDCEEGEI NNRVKKCVPI VSDVKVFLNQ FNQKFQREIF QKKSDWYNYI EDLRFKWPDT
RELNTAGINP NVFMHQLSKA SVATKAYLAD VGAHQMWAAQ SIEINNKQLF LTSGGMGAMG
FALPASIGAC LALNVSPVVT IIGDGCMQIN IQELQTIVRN KLPIKIVVMN NQNLGMIRQF
QDSYFESRYQ STWWGYSAPD FEKVAMAYGI PAKTVTNELE ILEAVNWMWN EENLSLPVLL
QVMIDPHTNT YPKIAFGKPI TEMEPFSKPI AMEST
//
