ID I4EW49_9ACTN Unreviewed; 572 AA.
AC I4EW49;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Dihydroxy-acid dehydratase (DAD) {ECO:0000313|EMBL:CCH87612.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:CCH87612.1};
GN OrderedLocusNames=MODMU_2177 {ECO:0000313|EMBL:CCH87612.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH87612.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH87612.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH87612.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; FO203431; CCH87612.1; -; Genomic_DNA.
DR AlphaFoldDB; I4EW49; -.
DR STRING; 477641.MODMU_2177; -.
DR KEGG; mmar:MODMU_2177; -.
DR PATRIC; fig|477641.3.peg.2071; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_3_1_11; -.
DR OMA; MMFRNLA; -.
DR Proteomes; UP000006461; 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 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; 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.
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:CCH87612.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006461}.
SQ SEQUENCE 572 AA; 60207 MW; 9549E2B891E7D613 CRC64;
MSAVALRSTQ WYSGDVRNAY IHRAWMRRGA PDDAFDRPQI AIANTASDLV PCNRHLTEVA
AAVRDGVHAA GGTPLELPVM GLGETQVRPT AMLWRNLAAM QMEEAFRANP VDGLVLLGGC
DKTIPSLLMA AASVDLPAVV VPGGPMLTGT FRGVPLGCGT DVFRLSEEVR AGTLSAEDFT
RSESAMIRSR GHCNTMGTAS TMALVAEALG TVVPGLAGTP AADSRLLEAA HGTGRLVVEM
VAADRRPSTF LTRASFANAI VALAAIGGST NAVVHLLAIA GRLGIDLTLD DFDRIGSGVP
VLVDLLPAGR FLMEDLHRAG GLLAVLGEVR DLLDPSALTV TGRPLVDHLD DAPVWDPEVI
RPRRAPLVDH GGIAVLRGNL APGGAVVKPA AASPHLMRHR GRAVVFDSIE DFHARIDDPD
LDVDADSVLV LRGCGPRGYP GMPEVANMPL PRKLLEQGVR DMVRVCDGRM SGTAYGTVVL
HVAPEAAAGG PLALVRTGDV ISLDVAARRI DVEVDDAELA ARTPSEATTA AFARPARGWE
RLYVDHVLQA DTGADLDFLR GSSGSQVSRE SH
//
