ID G2NGY6_STREK Unreviewed; 579 AA.
AC G2NGY6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:AEN09240.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:AEN09240.1};
GN ORFNames=SACTE_1320 {ECO:0000313|EMBL:AEN09240.1};
OS Streptomyces sp. (strain SirexAA-E / ActE).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN09240.1, ECO:0000313|Proteomes:UP000001397};
RN [1] {ECO:0000313|EMBL:AEN09240.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA Adams S., Book A., Currie C., Woyke T.;
RT "Complete sequence of Streptomyces sp. SirexAA-E.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEN09240.1, ECO:0000313|Proteomes:UP000001397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA Book A.J., Currie C.R., Fox B.G.;
RT "Biochemical properties and atomic resolution structure of a
RT proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT SirexAA-E.";
RL PLoS ONE 9:e94166-E94166(2014).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002993; AEN09240.1; -; Genomic_DNA.
DR RefSeq; WP_014045228.1; NC_015953.1.
DR AlphaFoldDB; G2NGY6; -.
DR STRING; 862751.SACTE_1320; -.
DR KEGG; ssx:SACTE_1320; -.
DR PATRIC; fig|862751.12.peg.1379; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_3_1_11; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000001397; 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:SF2; DIHYDROXY-ACID DEHYDRATASE; 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:AEN09240.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001397}.
SQ SEQUENCE 579 AA; 62693 MW; CA9A52A92CE73EE7 CRC64;
MTEDTGRRIA PEELRSHQWY GADGLRSFSH RARTRQLGYL PEEHLGKPVV AILNTWSDIN
PCHVHLRDRA QAVKRGVWQA GGFPLEFPVS TLSETFQKPT PMLYRNMLAM ETEELLRSYP
VDGAVLLGGC DKSTPALLMG AASVDLPTVF VPAGPMLPGH WRNEVLGSGT DMWKYWDDKR
AGLIGDCEMG ELENGLARSP GHCMTMGTAS TLTAAAEALG VTVPGASSIP AVDSGHDRMA
ARSGLRIVEL VWQQLTLSKI LTADAYEDAV ATVLALGGST NAVIHLIAMA GRSGVKLTLD
DFDRIARTVP VLADLRPGGR YLMEDFHFAG GLPGFLARLT DVLHLDRPTV AHTTLREQIE
GALVHNADVI RERGNPLAEE GGVAVLRGNL CPDGAVIKHI AAEPHLLRHT GPAVVFDDYK
EMQRTINDPA LALTPDHVLV LRNAGPKGGP GMPEYGMLPI PDYLLKQGVR DMVRLSDARM
SGTSYGACVL HIAPESFVGG PLALVRTGDL VTLDVEARLL HLDVTDEELE ERRAAWTPPP
ARYGRGYGAL YQDQITQADT GCDFTFLARP GEVPDPYAG
//