ID F2IWW4_POLGS Unreviewed; 584 AA.
AC F2IWW4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Acetolactate synthase large subunit {ECO:0000313|EMBL:ADZ71541.1};
GN OrderedLocusNames=SL003B_3119 {ECO:0000313|EMBL:ADZ71541.1};
OS Polymorphum gilvum (strain LMG 25793 / CGMCC 1.9160 / SL003B-26A1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Polymorphum.
OX NCBI_TaxID=991905 {ECO:0000313|EMBL:ADZ71541.1, ECO:0000313|Proteomes:UP000008130};
RN [1] {ECO:0000313|EMBL:ADZ71541.1, ECO:0000313|Proteomes:UP000008130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25793 / CGMCC 1.9160 / SL003B-26A1
RC {ECO:0000313|Proteomes:UP000008130};
RX PubMed=21478361; DOI=10.1128/JB.00333-11;
RA Li S.G., Tang Y.Q., Nie Y., Cai M., Wu X.L.;
RT "Complete genome sequence of Polymorphum gilvum SL003B-26A1T, a crude oil-
RT degrading bacterium from oil-polluted saline soil.";
RL J. Bacteriol. 193:2894-2895(2011).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002568; ADZ71541.1; -; Genomic_DNA.
DR RefSeq; WP_013653852.1; NC_015259.1.
DR AlphaFoldDB; F2IWW4; -.
DR STRING; 991905.SL003B_3119; -.
DR KEGG; pgv:SL003B_3119; -.
DR PATRIC; fig|991905.3.peg.3204; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_4_0_5; -.
DR OrthoDB; 7534569at2; -.
DR Proteomes; UP000008130; 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; cd02002; TPP_BFDC; 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:SF13; ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL; 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:UP000008130};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 24..153
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 227..352
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 433..576
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 584 AA; 61940 MW; DCC34EC1A336D814 CRC64;
MQKATPSPTG TAAGAGRAES ASLTTGGALL ARLKALGIDY IFANSGTDFP PIIEGLAEAE
AKQIELPQGL VMPHEAAAMG MAHGYYLATG RTQAVMAHTN VGLANCAIGA INAATEHIPV
LLFSGRTPTT EKGRLGSRTV PIGWGQEMHD QTALVREACK WDYELRFPEQ VSEIVDRALA
IAETTPRGPV YISLPREVLC EPCATDGIAA PASIRPARPG LDAAAFDEAA RLIASARNPV
IFAQRGTGGE AGFAALAEIA SDWGAPVCQY WAVRLALPLD HPMAAAPDPA PLLAEADVVL
VIDSLAPWSP DIHKLRPGCK VIHLGQDPLY TRFPVRNFPC DLALACDVEP GLLALRDRLA
PVKDVRASDI AARRDAWAAR NAASRQAVLA RAEQGRSDPM TKDWVSLCLS RALEGRDAAV
LSELGCPLAP MTLAHPKSWY QEPHSGGLGW SFPAALGMKL GNRDRTVVAT MGDGSYIFSN
PVACHQIAEA LDLPILVLVV NNAEWGAVRQ SVLGLYPDGH AARSNKMPLT QLAPVPDFVR
VAEASRAYAR RVDHGDALPQ ALAEALGHID SKGTLALLDV RVRA
//
