ID G8RNF5_MYCRN Unreviewed; 575 AA.
AC G8RNF5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=acetolactate synthase {ECO:0000256|ARBA:ARBA00013145};
DE EC=2.2.1.6 {ECO:0000256|ARBA:ARBA00013145};
GN OrderedLocusNames=MycrhN_0652 {ECO:0000313|EMBL:AEV71287.1};
OS Mycolicibacterium rhodesiae (strain NBB3) (Mycobacterium rhodesiae).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV71287.1, ECO:0000313|Proteomes:UP000005442};
RN [1] {ECO:0000313|EMBL:AEV71287.1, ECO:0000313|Proteomes:UP000005442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBB3 {ECO:0000313|EMBL:AEV71287.1,
RC ECO:0000313|Proteomes:UP000005442};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A.,
RA Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2;
CC Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000673};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004974}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 1/4. {ECO:0000256|ARBA:ARBA00005025}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP003169; AEV71287.1; -; Genomic_DNA.
DR RefSeq; WP_014209105.1; NC_016604.1.
DR AlphaFoldDB; G8RNF5; -.
DR STRING; 710685.MycrhN_0652; -.
DR KEGG; mrh:MycrhN_0652; -.
DR PATRIC; fig|710685.3.peg.659; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_1_11; -.
DR OrthoDB; 2254214at2; -.
DR UniPathway; UPA00047; UER00055.
DR UniPathway; UPA00049; UER00059.
DR Proteomes; UP000005442; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
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: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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Ligase {ECO:0000313|EMBL:AEV71287.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005442};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..294
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 386..538
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 575 AA; 59747 MW; 44D0AC9E931FFECD CRC64;
MARHRVVDHI VGYLAAAGVD HIFGVDGANI EDLYDAAHYR ADITAVLAKH EFSAATMADG
YSRSGAGLGV VAATSGGGCL NTVPGLGEAL ASRVPVLALI GQAPMSLDGR GSFQDTSGRN
GALDAQALFS AVSVYCKRVL TPQDILTALP EAIAAARTGG PAVLLLPKDI QQATLDVVNG
SAVPVGRRNA HVGNPHPIAR ALQNVDGPVT IIAGEQVARD DARAELERLR SLLRARVACV
PDAKDVAGTP GMGSSSAVGV TGVMGHPGVA DAISESALCL VVGTRMTVTA RGGLDDALRS
ARVYSIGAET PYLPCTHVHT EDLRASLSLL TSALSGHGRP ARVRVPDAVR RSELRPPAHD
CPGIRYRDAL TVLDRALPDG TDIVVDAGNI GASAIHHLPV RRGGRFIVAL GMGGMGYSFG
AGIGMTFGRG ADSADRTVVI AGDGSFFMHG MEIHTALQYR LPITFVLFDN HAHAMCVTRE
QVFYGDQYSY NRFGPSRLGA GLAAMFPELR SVDVDDIGAL PAALAGALDV QGPSVISIEC
SADEIPPFAA FLGNAADAVS QPHIEKDHRN VAARA
//
