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Database: UniProt
Entry: A0A010ZSW8_9ACTN
LinkDB: A0A010ZSW8_9ACTN
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ID   A0A010ZSW8_9ACTN        Unreviewed;       619 AA.
AC   A0A010ZSW8;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:EXG81769.1};
GN   ORFNames=CryarDRAFT_2889 {ECO:0000313|EMBL:EXG81769.1};
OS   Cryptosporangium arvum DSM 44712.
OC   Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC   Cryptosporangiaceae; Cryptosporangium.
OX   NCBI_TaxID=927661 {ECO:0000313|EMBL:EXG81769.1, ECO:0000313|Proteomes:UP000021053};
RN   [1] {ECO:0000313|EMBL:EXG81769.1, ECO:0000313|Proteomes:UP000021053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44712 {ECO:0000313|EMBL:EXG81769.1,
RC   ECO:0000313|Proteomes:UP000021053};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (JUL-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:EXG81769.1}.
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DR   EMBL; JFBT01000001; EXG81769.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A010ZSW8; -.
DR   PATRIC; fig|927661.3.peg.2851; -.
DR   HOGENOM; CLU_013748_6_0_11; -.
DR   OrthoDB; 3194735at2; -.
DR   Proteomes; UP000021053; Unassembled WGS sequence.
DR   GO; GO:0016823; F:hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances; 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:0019310; P:inositol catabolic 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; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR030817; Myo_inos_IolD.
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; TIGR04377; myo_inos_iolD; 1.
DR   PANTHER; PTHR18968:SF9; 3D-(3,5/4)-TRIHYDROXYCYCLOHEXANE-1,2-DIONE HYDROLASE; 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:UP000021053};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          4..123
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          217..350
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          408..566
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   619 AA;  65698 MW;  24079B411C800A92 CRC64;
     MKLTVAQATV RFLAAQYSER DGVRQRLIAG CLGIFGHGNV AGLGQALLQD PDLLPYVLGR
     NEQAMVHTAV AYARMKDRLQ TYAVSTSIGP GATNMITGAA LATVNRLPVL LLPADTFADR
     SAAPLLQELE VPWSGDVTVN DAFRPVSKYF DRVHRPEQLP AALLAAMRVL TDPAETGAVT
     ICLPQDVQAQ AFDWPDEFFA DRVWRVARPV PEPGDLAEAG ALIRSARRPL IVAGGGVGYS
     GAHAALARFC ESTGIPVGLT QAGKGALPFD HEQCLGAIGS TGTAAANTIA AEADLVIGVG
     TRYSDFTTAS RTAFGADGVR FVNVNVAGLD AVKHAGLAVR ADARTTLEAL AGLEYTVAPE
     YRAEYTRLDA EWNARVRAAY DTEELTQSAV IGAVNDLSDP RDVVVCAAGS MPGDLHKLWQ
     TRDAKGYHVE YGYSCMGYEI AGGLGVALAC PDRDVFVLVG DGSYLMMATE LVTALQEDLK
     VIVVLVQNHG FASIGALSES LGSQRFGTRY RYRTKSGRLD GDLLPVDLAA NAASLGVPVV
     RVEDRAALAD AIAAAKASAT STLIHVETDP FHNGAPDTGA WWDVPVSEVS TLDSTQAAYR
     TYAEHKATQR TYLHPTEAS
//
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