ID A0A348B4G1_9CREN Unreviewed; 332 AA.
AC A0A348B4G1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Ketol-acid reductoisomerase {ECO:0000313|EMBL:BBD73063.1};
GN ORFNames=GCM10007116_20980 {ECO:0000313|EMBL:GGU03981.1},
GN HS1genome_1452 {ECO:0000313|EMBL:BBD73063.1};
OS Sulfodiicoccus acidiphilus.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfodiicoccus.
OX NCBI_TaxID=1670455 {ECO:0000313|EMBL:BBD73063.1, ECO:0000313|Proteomes:UP000276741};
RN [1] {ECO:0000313|Proteomes:UP000276741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS-1 {ECO:0000313|Proteomes:UP000276741};
RA Sakai H.D., Kurosawa N.;
RT "Complete genome sequence of Sulfodiicoccus acidiphilus strain HS-1.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BBD73063.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HS-1 {ECO:0000313|EMBL:BBD73063.1};
RX PubMed=31331368;
RA Sakai H.D., Kurosawa N.;
RT "Complete genome sequence of the Sulfodiicoccus acidiphilus strain HS-1T,
RT the first crenarchaeon that lacks polB3, isolated from an acidic hot spring
RT in Ohwaku-dani, Hakone, Japan.";
RL BMC Res. Notes 12:444-444(2019).
RN [3] {ECO:0000313|EMBL:GGU03981.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 31740 {ECO:0000313|EMBL:GGU03981.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [4] {ECO:0000313|EMBL:GGU03981.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 31740 {ECO:0000313|EMBL:GGU03981.1};
RA Sun Q., Ohkuma M.;
RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004885}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 2/4. {ECO:0000256|ARBA:ARBA00004864}.
CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC {ECO:0000256|ARBA:ARBA00010318, ECO:0000256|PROSITE-ProRule:PRU01198}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01198}.
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DR EMBL; AP018553; BBD73063.1; -; Genomic_DNA.
DR EMBL; BMQS01000027; GGU03981.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A348B4G1; -.
DR KEGG; sacd:HS1genome_1452; -.
DR OrthoDB; 6064at2157; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR Proteomes; UP000276741; Chromosome.
DR Proteomes; UP000616143; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 6.10.240.10; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013023; KARI.
DR InterPro; IPR000506; KARI_C.
DR InterPro; IPR013116; KARI_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR21371; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR21371:SF1; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR Pfam; PF01450; IlvC; 1.
DR Pfam; PF07991; IlvN; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51851; KARI_C; 1.
DR PROSITE; PS51850; KARI_N; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PROSITE-ProRule:PRU01198};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|PROSITE-ProRule:PRU01198};
KW Isomerase {ECO:0000313|EMBL:BBD73063.1};
KW Magnesium {ECO:0000256|PROSITE-ProRule:PRU01198};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01198};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|PROSITE-
KW ProRule:PRU01198}; Reference proteome {ECO:0000313|Proteomes:UP000276741}.
FT DOMAIN 1..183
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000259|PROSITE:PS51850"
FT DOMAIN 186..332
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000259|PROSITE:PS51851"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
SQ SEQUENCE 332 AA; 36542 MW; 64F3B44C9F048916 CRC64;
MKDSIVFDAD LSPLRGTTLA VVGYGNQGSA QAKILRASGL DVIVGNVRDS YWEKAERDGF
KVYDIPEAVE RAQGALLLVP DEVMPQVFKE KVEPSIKGKD DFLLDFASGY NVAFGFVRPP
SNADVVMVAP RMIGWGVTEL HSKGMGYPVL VGVEQDASGA AWERALALAK GVGAIGLPGG
VAVKSSFQEE ALLDLMSEHT WVPVLFAAIK ACFDVAVEEY GVSPAAALLE FYASGELAEI
AQLMAQEGIF EQMKHHSTTS QYGTLTRFYK YYDQVRELVE GEAAQIWSGE FAREWSLEQQ
AGTPVFSRLW RLARESSMSK EEHELYRALK RR
//
