ID A0A1H7YAE3_9RHOB Unreviewed; 536 AA.
AC A0A1H7YAE3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SEM42925.1};
GN ORFNames=SAMN04488103_101127 {ECO:0000313|EMBL:SEM42925.1};
OS Gemmobacter aquatilis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Gemmobacter.
OX NCBI_TaxID=933059 {ECO:0000313|EMBL:SEM42925.1, ECO:0000313|Proteomes:UP000198761};
RN [1] {ECO:0000313|EMBL:SEM42925.1, ECO:0000313|Proteomes:UP000198761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3857 {ECO:0000313|EMBL:SEM42925.1,
RC ECO:0000313|Proteomes:UP000198761};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOCE01000001; SEM42925.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7YAE3; -.
DR STRING; 933059.SAMN04488103_101127; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000198761; 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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000198761};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 9..124
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 195..326
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..523
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 536 AA; 54563 MW; FBD5B8757D48CEDC CRC64;
MGNSGISTGV YLTHLLRAYG VEVVFGIPGV HTVELYRGLA GSGIRHVTPR HEQGAGFMAD
GYARASRKPG VCFIISGPGM TNILTAMGQA HADSVPMLVI STVNAHGRMG SGQGWLHEMP
DQSATVAGVA AFSRTIHRPE DLAPAVAQAF ALFASARPRP VHLELPINVM LAEAGHLPVP
APLRLSRPAP DPAMVAEAAS LLNNARKTVI LAGGGAAHAT LAPLAEALDA PVVMTTNARG
LLPPGHPLAV SLSPSLPATR ALIAAADVVL ALGTEMGSTD YDMYEDGGFP PPARLIRVDL
DPLQIARGLP ATLGIVADAA LTVAALTAAL PPRPPGDGAA RAAAAQAGRA GLSVDMQGDL
RILDLVRDTL PAARLVGDST QLTYAGNLGF AAATAGSWFN SATGFGTLGY GLPAAIGAKL
ADARPVVAIS GDGGLQFVLG ELASAAEAQV PVILLLHDNN GYGEIKSYMI SKNIPPLGVD
ILTPDLAAIA AACGWQVARV TDLDALPGLL RQGAAAGGPT LLIFGDDLRA QAAARA
//
