ID A0A238YGB7_9RHOB Unreviewed; 585 AA.
AC A0A238YGB7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Acetolactate synthase-1/2/3 large subunit {ECO:0000313|EMBL:SNR70110.1};
GN ORFNames=SAMN06265378_11830 {ECO:0000313|EMBL:SNR70110.1};
OS Paracoccus sediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1214787 {ECO:0000313|EMBL:SNR70110.1, ECO:0000313|Proteomes:UP000198409};
RN [1] {ECO:0000313|Proteomes:UP000198409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26170 {ECO:0000313|Proteomes:UP000198409};
RA Varghese N., Submissions S.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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; FZNM01000018; SNR70110.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238YGB7; -.
DR Proteomes; UP000198409; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd02004; TPP_BZL_OCoD_HPCL; 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:SF166; 2-HYDROXYACYL-COA LYASE 2; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 23..130
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 212..337
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 418..547
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 358..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 585 AA; 61790 MW; 4B99A0ECB3F07755 CRC64;
MNLQTGQAPG SVQDLNGDPH SCAAWVAQFL KARGIDRIFG LQGGHIQPIW DHCARLGIRI
VDCRHEGAAV HMAHAHAELA GTLGVAVVTA GPGVTNTVTA IANASLARVP VLVIGGCTSR
PQANMGPLQD IPHVDIIRPV ARYCRTARVA DQVIRELDEA VARAMGDLGE PGPSYIEIPT
DVLRTHVAPD LVLDDWMAPK PARRIPPDPG AVAQAVQAIL AAKRPLVVTG RGARGAAPEL
LRLLDATGAL YLDTQESRGL VPPDHPSGVG AMRGVVLGEA DLVIVVGRKL DYQLGYGSPA
VYPRARFIRI SDNAGELIDN RRGAPEILAD PALALAAVTD ALGNQATALD RPWAEGLRAR
HLSRSSPDTR RETPGRSEDG KVHPAAIFDA IRDVADPDYI AIADGGDLLS FARVGLEAKT
YLDAGAFGCL GVGVPFAVAA SLACPDRQVI SISGDGAFGL NAMEIDTAVR HGAKAVFIVS
NNAAWNIERH DQAENYGGRV VGTLLRHSDY AAMARALGLH AERVEDPADL PGALRRALDN
APALIDVVTS QSAVSSDARK GLGFVPDYQP LTAWDDAERR RRGLP
//
