ID A0A1G8RP92_9EURY Unreviewed; 547 AA.
AC A0A1G8RP92;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acetolactate synthase, large subunit {ECO:0000313|EMBL:SDJ18894.1};
GN ORFNames=SAMN05216226_10140 {ECO:0000313|EMBL:SDJ18894.1};
OS Halovenus aranensis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halovenus.
OX NCBI_TaxID=890420 {ECO:0000313|EMBL:SDJ18894.1, ECO:0000313|Proteomes:UP000198856};
RN [1] {ECO:0000313|EMBL:SDJ18894.1, ECO:0000313|Proteomes:UP000198856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M10015 {ECO:0000313|EMBL:SDJ18894.1,
RC ECO:0000313|Proteomes:UP000198856};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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; FNFC01000001; SDJ18894.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8RP92; -.
DR STRING; 890420.SAMN05216226_10140; -.
DR OrthoDB; 6837at2157; -.
DR Proteomes; UP000198856; 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 GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR CDD; cd00568; TPP_enzymes; 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:SF167; 2-KETOARGININE DECARBOXYLASE ARUI-RELATED; 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:UP000198856};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 1..111
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..321
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..531
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 524..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 547 AA; 56835 MW; DCBAFC6658E7144C CRC64;
MKVGRAVIER LAENGIDTLF GIPGKQTLPL NEAIGNRDDI DFVVARHETA VSHAAWGYAE
TSGRPAATVV IPGPGDMNAM NGLKNALNDC TPLVHIAVET SPEIRGGDGI HETPPDTYDN
VVKTNTVVDS PESTLVELQQ AIDTAMTPPK GPVRVGIPKN FLKQDVALAT PATYSREYTT
DVPAEDVAAG ADLLASSSEP VILAGGGVRA SGGSDRLRAV AEALNAPIVT TYKGKGAVPD
SDDRVAGALS GSASPELLDC LAEADAMLAV GTDFDAVATR AWSVEVPEAL VHVTLSPDDL
GTGYDPTVGI VADATAALDA LATELDDRTT PDGNGIERAT AVRAGTADRI EPLLGEEPPL
TSVQALRTVR EAIPEETVVA ADAGGFRVWG LNVFEAAGPR SYVNPGSWAT MGTGLPSGLG
AQLANPDDDV VVLTGDGGLM MCLHELHTAV SEEIPVTVLV FNNSDYAIIS EEAGRSFDLP
EEAYSWADAP LDFATIADGM GLETAQASRP DEIAAELTDA LDTDAPTLLE VPTDPTEPQA
STWMSSD
//
