ID M7XT60_9BACT Unreviewed; 574 AA.
AC M7XT60;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:EMS31692.1};
GN ORFNames=C943_01963 {ECO:0000313|EMBL:EMS31692.1};
OS Mariniradius saccharolyticus AK6.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Mariniradius.
OX NCBI_TaxID=1239962 {ECO:0000313|EMBL:EMS31692.1, ECO:0000313|Proteomes:UP000010953};
RN [1] {ECO:0000313|EMBL:EMS31692.1, ECO:0000313|Proteomes:UP000010953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK6 {ECO:0000313|EMBL:EMS31692.1,
RC ECO:0000313|Proteomes:UP000010953};
RA Vaidya B., Khatri I., Tanuku N.R.S., Subramanian S., Pinnaka A.;
RT "Genome assembly of Mariniradius saccharolyticus AK6.";
RL Submitted (JAN-2013) 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}.
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:EMS31692.1}.
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DR EMBL; AMZY02000018; EMS31692.1; -; Genomic_DNA.
DR RefSeq; WP_008630407.1; NZ_AMZY02000018.1.
DR AlphaFoldDB; M7XT60; -.
DR STRING; 1239962.C943_01963; -.
DR eggNOG; COG0028; Bacteria.
DR InParanoid; M7XT60; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000010953; 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:UP000010953};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 225..350
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 412..552
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 574 AA; 61728 MW; C0A976FB8FB525E8 CRC64;
MNGGQIIAKV LQNHGVKFLF TLCGGHISPI FVGAEQLGIR VIDTRHEATA VFAADAVARL
TGVPGVAAVT AGPGITNAIT AVKNAQMAQS PLILLGGAAA TLLKGRGALQ DIDQISLLKP
IVKWAVSIGQ VKDIATVMEK AFRIAQSGTP GPVFIECPID TLYPKEMVLE WYGAKNQKGP
AGISASLKQW YIRRHANQLF KDSEKVAFET KPEQVQVPNF SQAQLEKAIR MVKKAKKPLM
ILGSGAMSQP KKVEDLASAV RKLGIPIYLS GMGRGLLGPD SDIQVRHKRK EAIKESDLII
LAGVPNDFRL DYGNHIGSRP FISIHRDIKE LMLNKKPTLP IKADPIDFLI AVSGHFAFEG
HQWISQLKQR DAARDGEIQA QSELPTSGLN PLDLLLNLKK NLDQNAVLIA DGGDFVATAS
YTLRPRGPLS WLDPGAFGTL GVGAGFAIGA ALVYPDRPIW VLFGDGSAGY SLTEFDTFQR
HGLRITALVG NDACWTQIAR DQVDFLGSDC AVNLEFSDYH LVPKAFGGDG IKIEAKGEIN
HAIEIAKASN ASGKSFLINA IIGKADFRKG SISV
//
