ID A0A0D7E6B8_RHOPL Unreviewed; 541 AA.
AC A0A0D7E6B8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Acetolactate synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=OO17_24765 {ECO:0000313|EMBL:KIZ36419.1};
OS Rhodopseudomonas palustris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=1076 {ECO:0000313|EMBL:KIZ36419.1, ECO:0000313|Proteomes:UP000032515};
RN [1] {ECO:0000313|EMBL:KIZ36419.1, ECO:0000313|Proteomes:UP000032515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL398 {ECO:0000313|EMBL:KIZ36419.1,
RC ECO:0000313|Proteomes:UP000032515};
RA Bentzon-Tilia M., Severin I., Hansen L.H., Riemann L.;
RT "Genomics and ecophysiology of heterotrophic nitrogen fixing bacteria
RT isolated from estuarine surface water.";
RL Submitted (NOV-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:KIZ36419.1}.
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DR EMBL; JXXE01000580; KIZ36419.1; -; Genomic_DNA.
DR RefSeq; WP_044416830.1; NZ_JXXE01000580.1.
DR AlphaFoldDB; A0A0D7E6B8; -.
DR PATRIC; fig|1076.23.peg.6069; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000032515; 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:0044281; P:small molecule metabolic 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; ACETOLACTATE SYNTHASE LARGE SUBUNIT ILVB2-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 Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..122
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..318
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 384..521
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 541 AA; 57511 MW; C72785C62D5816E1 CRC64;
MTAMTGGEAI VQGLKAHGVD TVFGLPGAQI YGLFDGFAKA QLKVVGARHE QACGYMAFGY
ARASGRPGVF SVVPGPGVLN AGAAMLTALG CNEPVLCLTG QVPTAFLGKG RGHLHEMPDQ
LATLRSFVKW AERIDYPDGA PTKVSRAFQE MMSGRRGPAA LEMPWDVFTQ RAEVAAVAPF
ARFAAPQPDP DRIKAAAALI AASKAPMIFV GGGAFDAAGE ILDLAELIDA PVVAFRSGRG
IVSNAHELGL TFAAAYNLWP QTDLIIGIGT RMELATMSRW PYRPEGQRSI RIDIDPSEMR
RFTPDAALIA DAQAGTSALA AAVRKQGYAK SATRRGEIRE ASVLAAQQIQ SVQPQMAYLN
ILREVLPDDA IVTDELSQVG FASWYGFPVY QPRTFITSGY QGTLGSGFPT ALGAKVAFPD
RPVVAITGDG GFMFAVQELA TAVQYNIGVV TLVFNNSAYG NVRRDQVNLF EGRAVASDLT
NPDFVRLAQS FGVGAARVTE PDQFKAALET ALADGGPYLI AIEVPKDSES SPWPFIHPAK
P
//