ID A0A3B7D1G6_9ACTN Unreviewed; 527 AA.
AC A0A3B7D1G6;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:AXT84156.1};
GN ORFNames=C6I20_02395 {ECO:0000313|EMBL:AXT84156.1};
OS Aeromicrobium sp. A1-2.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Aeromicrobium.
OX NCBI_TaxID=2107713 {ECO:0000313|EMBL:AXT84156.1, ECO:0000313|Proteomes:UP000257855};
RN [1] {ECO:0000313|EMBL:AXT84156.1, ECO:0000313|Proteomes:UP000257855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1-2 {ECO:0000313|EMBL:AXT84156.1,
RC ECO:0000313|Proteomes:UP000257855};
RA Liao L., Chen B.;
RT "Complete genome of Aeromicrobium sp. A1-2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP027482; AXT84156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B7D1G6; -.
DR KEGG; aeb:C6I20_02395; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000257855; Chromosome.
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; 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:UP000257855};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..321
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..522
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 527 AA; 54429 MW; F4F0C8A04F64379B CRC64;
MAIMTGGEAV ARSLAAHGAD VVFGIPGNHN LPIYEHLASN DIRHFLSRHE QGCGFGADGY
ARVTGRPGIA LVTAGPAVLN TLAALSQSYA DSVPVLMVSP GMPLRHPFGG NGHLHEVKDQ
QAAVDAVVSV SHRVSSVDEI GDAITQAYSD MTAGRPRPVH VEIPIDVLDE VADTEVGMPL
ALPTVSAPQG ELTRAAAVLA ESSRPGIVVG GGARAASAEV LALAEKLGAS VVTTTNGKGI
LPEDHRLSLG AGAHLASVGE WVRSRDVLLA VGTDFGPSDL WNGPWTIDGT LVRIDIDPRQ
IGVNVRPDIA LVSDAAAALG SLVDLIGDRH ETSDGEALAW AARAHEESAS EGALWADEMK
AMSDVLDRNA IVAGDSAAVC YYGLRANLPL HTPGAFLYPT GSGTLGYGLP AAIGAKVAAP
DRQVVAVMGD GGVMFTLPEI AAAAAEGMAL PLIVIDNGGY GQIRKNMNLR GYDPLGVDFP
SPDFAAAGRA LGCYGMSIES PEQLSEELAK ALVADRPTVL HVKEGRA
//
