ID B9NW09_9RHOB Unreviewed; 557 AA.
AC B9NW09;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Putative acetolactate synthasecatabolic {ECO:0000313|EMBL:EEE35915.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:EEE35915.1};
GN ORFNames=RKLH11_3516 {ECO:0000313|EMBL:EEE35915.1};
OS Rhodobacteraceae bacterium KLH11.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=467661 {ECO:0000313|EMBL:EEE35915.1, ECO:0000313|Proteomes:UP000005135};
RN [1] {ECO:0000313|Proteomes:UP000005135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLH11 {ECO:0000313|Proteomes:UP000005135};
RX PubMed=21742885; DOI=10.1128/jb.05556-11;
RA Zan J., Fricke W.F., Fuqua C., Ravel J., Hill R.T.;
RT "Genome Sequence of Ruegeria sp. Strain KLH11, an N-Acylhomoserine Lactone-
RT Producing Bacterium Isolated from the Marine Sponge Mycale laxissima.";
RL J. Bacteriol. 193:5011-5012(2011).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; DS999532; EEE35915.1; -; Genomic_DNA.
DR AlphaFoldDB; B9NW09; -.
DR STRING; 467661.RKLH11_3516; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_2_5; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000005135; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR CDD; cd02010; TPP_ALS; 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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000005135};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:EEE35915.1}.
FT DOMAIN 13..127
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..330
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 389..535
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 557 AA; 60915 MW; 03F952A6684CF24D CRC64;
MTSPDTPAQR LSKASDLLVS SLEAEGVEHI FAVPGEENLD VVESLRTSSI ELVLTRHEQG
AAFMAATYGR LTGKAGVCMA TLGPGATNFA TPAAYANLGG MPLIMITGQK PIKKSKQGQF
QIVDIVNLFE PICKMSKQIV HGNTIPALVR EAFRVAEEER PGAVLLELPE DIAAEEVDAH
VLQPHPRHYA IAGDTVLAEA AEMIKSAKMP LLLLGAGANR QHARSALSKF IEDTRIPFFN
TQMGKGVVDE RSELFLGTAA LSDGDYVHCA IDRADLIINV GHDVVEKPPF FMEENGTKVI
HVNYKAAQVD QVYFPQIEVV GDIAQSITRL GDILGGALEF DRSYYMRIKQ ETDLHTSEGS
DDARFPIVPQ RFVADTRKVM GDQDIIALDN GIYKIWYARN YKAYQPNTIL LDNALATMGA
GLPSAMMASM LYPDRRVMAI CGDGGFMMNS QEVETAVRLG LNLVITVLDD SSYGMIRWKQ
AHAGFADWGL EFNNPDFVQH ANSYGATGHR VERTEDLVPT FEKAFAAGGV HLVDVPVDYS
ENQRVLIDEL AAKTCLI
//