ID A0A2R8ARG6_9RHOB Unreviewed; 551 AA.
AC A0A2R8ARG6;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Acetolactate synthase isozyme 2 large subunit {ECO:0000313|EMBL:SPF78653.1};
DE EC=2.2.1.6 {ECO:0000313|EMBL:SPF78653.1};
GN Name=ilvG {ECO:0000313|EMBL:SPF78653.1};
GN ORFNames=ALP8811_02582 {ECO:0000313|EMBL:SPF78653.1};
OS Aliiroseovarius pelagivivens.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Aliiroseovarius.
OX NCBI_TaxID=1639690 {ECO:0000313|EMBL:SPF78653.1, ECO:0000313|Proteomes:UP000244911};
RN [1] {ECO:0000313|EMBL:SPF78653.1, ECO:0000313|Proteomes:UP000244911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8811 {ECO:0000313|EMBL:SPF78653.1,
RC ECO:0000313|Proteomes:UP000244911};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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; OMOI01000002; SPF78653.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8ARG6; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000244911; Unassembled WGS sequence.
DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC.
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:SF120; ACETOLACTATE SYNTHASE LARGE SUBUNIT; 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:UP000244911};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132};
KW Transferase {ECO:0000313|EMBL:SPF78653.1}.
FT DOMAIN 3..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..323
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..527
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 551 AA; 58815 MW; F6DAB4C7790F9E77 CRC64;
MRHGGQILVD HLKTEGVSRV FSVPGESFLA ALDGLYDSGI ENVVCRQEGG AAMMAEAHGK
LTGAPGVLFV TRGPGATNAS SGIHVAMQDA TPMVVFVGQI ARAHRDRGAF QEVDYRAFFG
PLAKWSCEVD QTERLPEYLA RAFHVARTGR PGPVVVALPE DMLSDVADVP DRPAVPATQG
RVSSADAGAM LAAIETSARP LLIAGGPGWT ADAGADLMAF AAQNALPVAT AFRRQDYVDN
RHPNYVGDLG LGINPALKTM FDEADTLVVL GSRLGDILTG SYEMLDPIHT GKRIVHVYPC
AEELGRVYHA DQTVLATGPA AIAALSEPPA LSATPWADWT QQGRAAYDAF QAPIETPGPV
KLERIMHWLS DTLPDNTIMT NGAGNYATWL HRYFRFKEYG TQLAPTSGSM GYGFPAAVAA
SLQHPDRTVI AWLGDGEFQM TLNEMSTAVQ HGAKPIAIIV NNGRYGTIRM HQERTYPARV
SGTDMANPEF ADLARAYGGH GETVTKGEDF EAAFQRAKAS GKLAVIDLEV DPQVATPGLT
LDQLRAQGEA G
//
