ID W5VZ66_9PSEU Unreviewed; 570 AA.
AC W5VZ66;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:AHH93867.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:AHH93867.1};
GN ORFNames=KALB_491 {ECO:0000313|EMBL:AHH93867.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH93867.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHH93867.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH93867.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; CP007155; AHH93867.1; -; Genomic_DNA.
DR RefSeq; WP_025354142.1; NZ_CP007155.1.
DR AlphaFoldDB; W5VZ66; -.
DR STRING; 1449976.KALB_491; -.
DR KEGG; kal:KALB_491; -.
DR PATRIC; fig|1449976.3.peg.498; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_3_1_11; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000019225; Chromosome.
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:AHH93867.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000019225}.
SQ SEQUENCE 570 AA; 60213 MW; EB39095FD25170F9 CRC64;
MVDSLRSHGW FRDEGVLGFT HRSWLRNQGH PDHAFDGRPV IGICQTASDL TPCNAHLRGL
AEHVRRGVYE AGGLPMEFPV TSLGEVLMRP TTMLFRNLVS MDVEETLRAN PLDGVVLLTG
CDKTTPALLM GAASVDLPTL VVNGGPMLNG RFRGRQLGSG TDVWRFADAR RTGAMSAADM
SAAEACMSRS AGHCNTMGTA STMACWVESM GLSLPGMGAL PAVDSRRAAL AHVSGSRIVE
LVREDVRLSA IATRQALENA VVVNAAIGGS SNFAVHLLAL AGRLGVPFGL DDVDRLGRDV
PLLVDLMPAG RHLMEDFCYA GGLPAVLREL GDRLPHPHAP TVTGGTLAEN TADAEVFDRE
VIRSVADPLR SDAGLAVLRG NLAPDGAVIK PAAASPRLLR HAGRAVVFHG VEDLHARIDT
VDCDADSVFV LTGVGPRGFP GMPEVGNFGL PKRLLDAGVD DAVRISDGRM SGTAFGTVVL
HVAPESAVGG PLALVRDGDL VELDVPARSL HLAVPEEELA RRRAEWTPPP RAAERGWVRL
YVDHVGQADT GVDLDFLVGG SGAPVPPGNH
//
