ID A0A109JVH9_9BRAD Unreviewed; 612 AA.
AC A0A109JVH9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:KWV55853.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:KWV55853.1};
GN ORFNames=AS156_05450 {ECO:0000313|EMBL:KWV55853.1};
OS Bradyrhizobium macuxiense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1755647 {ECO:0000313|EMBL:KWV55853.1, ECO:0000313|Proteomes:UP000057737};
RN [1] {ECO:0000313|EMBL:KWV55853.1, ECO:0000313|Proteomes:UP000057737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR 10303 {ECO:0000313|EMBL:KWV55853.1,
RC ECO:0000313|Proteomes:UP000057737};
RA Zelli J.E., Simoes-Araujo J.L., Barauna A.C., Silva K.;
RT "Draft Genome Sequence of the Strain BR 10303 (Bradyrhizobium sp.) isolated
RT from nodules of Centrolobium paraense.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KWV55853.1}.
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DR EMBL; LNCU01000060; KWV55853.1; -; Genomic_DNA.
DR RefSeq; WP_066507135.1; NZ_LNCU01000060.1.
DR AlphaFoldDB; A0A109JVH9; -.
DR OrthoDB; 7793094at2; -.
DR Proteomes; UP000057737; Unassembled WGS sequence.
DR GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR Gene3D; 3.50.30.80; IlvD/EDD C-terminal domain-like; 1.
DR InterPro; IPR042096; Dihydro-acid_dehy_C.
DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR InterPro; IPR037237; IlvD/EDD_N.
DR PANTHER; PTHR43183:SF1; HYPOTHETICAL DIHYDROXY-ACID DEHYDRATASE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR43183; HYPOTHETICAL DIHYDROXYACID DEHYDRATASE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00920; ILVD_EDD; 1.
DR SUPFAM; SSF143975; IlvD/EDD N-terminal domain-like; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR PROSITE; PS00886; ILVD_EDD_1; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KWV55853.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 66363 MW; 2C06640B92B33D59 CRC64;
MTKPHTNGHS AAGQDHKGKG RKLRSQEWFN NPHNPGMTAL YLERYLNYGL TREELQSGKP
IIGIAQTGND LSPCNRHHLE LAHRVREGIR AAGGIAMEFP THPIQETGKR PTAALDRNLA
YLGLVEILFG YPLDGVVLTT GCDKTTPACM MAAATVNLPA IVLSGGPMLN GWHEGQRTGS
GTVVWKARER LAAGEINYEQ FIEIVASSAP SVGHCNTMGT ASTMNSLAEA LGFSLPGCAA
IPAPYRERGQ IAYETGKRIV DMVWEDLKPS DFLTRQAFEN CIVVNSAIGG STNAPIHINA
LARHVGVELS IDDWQKYGHD VPLLVNMQPA GFYLGEEYHR AGGVPSVVRE LIKHKRIHEG
ALTVNGRTMG ENCKDAPAPD SDVIWSYDKP LVKDAGFIVL RGNLFDSAIM KTSVISKEFR
DRYLSNPKDI NAFEGRAIVF EGPEDYHERI EDPALNIDEH CVLFIRGTGP IGYPGGAEVV
NMQPPAALIK RGILSLPCIG DGRQSGTSGS PSILNASPEA AADGGLAILR TGDKVRIDLN
KGSANILISE DELRTRRAEL KAKGGFPHPA NQTPWQELYR QTVGQHATGA CLELATRYQD
IAGKMGVARD NH
//
