ID A0A023BSV9_9FLAO Unreviewed; 544 AA.
AC A0A023BSV9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Acetolactate synthase {ECO:0000313|EMBL:EZH72918.1};
GN ORFNames=ATO12_22580 {ECO:0000313|EMBL:EZH72918.1};
OS Aquimarina atlantica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aquimarina.
OX NCBI_TaxID=1317122 {ECO:0000313|EMBL:EZH72918.1, ECO:0000313|Proteomes:UP000023541};
RN [1] {ECO:0000313|EMBL:EZH72918.1, ECO:0000313|Proteomes:UP000023541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-S11-z7 {ECO:0000313|EMBL:EZH72918.1,
RC ECO:0000313|Proteomes:UP000023541};
RA Lai Q.;
RT "Aquimarina sp. 22II-S11-z7 Genome Sequencing.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:EZH72918.1}.
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DR EMBL; AQRA01000007; EZH72918.1; -; Genomic_DNA.
DR RefSeq; WP_034244407.1; NZ_AQRA01000007.1.
DR AlphaFoldDB; A0A023BSV9; -.
DR STRING; 1317122.ATO12_22580; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000023541; 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; 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:UP000023541};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 195..318
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 384..522
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 544 AA; 60057 MW; 33139E6C880E4083 CRC64;
MAKLTGGQIV VRSLIKQGVK IVFGLPGVQN DWLYNAFYDY QDEITVIHTR HEQGVGYMAL
GYYLASGKTA VYNVVPGPGF LNSSAALLTA YGLNAKVLAL VGQTPLKTQG KGWGVLHESK
DQLGIMKRLT KYSDKVNDIK EIPHKIQKSF QEMETGRPQP VGLEISMDLL MSSDEMAFPA
LEKEKQEIEI DTSIVNRIAE ALIHAKNPLI FVGSGAMDAS EEITALANYM QIPVFAYRTG
KGIVSSRNYL SHPVPAAYEL WKEADVVVGI GSHVRMPILK WGTDEHLSFI SVNIDINDHD
KIMTPNIALT ANAAQASKAI LETLKNKIPQ RTSREKEMQV LKASWKEKTA YLEPQATYLR
IIREELPDDG IFVDELTQVG FASRMLWEAY APRTYLSTGY MGTLGWGFPT ALGAKIAKPE
LPVITVCGDG GFMFAVQELA TAVQHKIGVI ICLFNNNAFG NVQNMQINNY GNKVIASDLT
NPDFIAMAES YGAHTEKVSD FDSFRQAIQK AKKQELPTLI EIGVGIDMPS TDQFKSMPKL
RGVN
//
