ID A0A430JL16_9BACL Unreviewed; 575 AA.
AC A0A430JL16;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:RTE11700.1};
GN ORFNames=EJQ19_00705 {ECO:0000313|EMBL:RTE11700.1};
OS Paenibacillus whitsoniae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2496558 {ECO:0000313|EMBL:RTE11700.1, ECO:0000313|Proteomes:UP000276128};
RN [1] {ECO:0000313|EMBL:RTE11700.1, ECO:0000313|Proteomes:UP000276128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MER 54 {ECO:0000313|EMBL:RTE11700.1,
RC ECO:0000313|Proteomes:UP000276128};
RA Seuylemezian A., Vaishampayan P.;
RT "Bacillus ochoae sp. nov., Paenibacillus whitsoniae sp. nov., Paenibacillus
RT spiritus sp. nov. Isolated from the Mars Exploration Rover during
RT spacecraft assembly.";
RL Submitted (DEC-2018) 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:RTE11700.1}.
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DR EMBL; RXHU01000004; RTE11700.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430JL16; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000276128; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; 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; 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 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000276128}.
SQ SEQUENCE 575 AA; 62259 MW; A5A7CFB8EAECB0E7 CRC64;
MSEQDDRSER GGQRRGEAFF NDTGLWGFIH RSFTKSMGYT DDDLKKPVIG ICNTFSELNK
CHSHFRELTE YVKRGVWQAG GLPMEFPTIS IGEPYVKPTT MLLRNLMAMD TEEMIKAHQI
DGVVLIGGCD KTVPAQLMAA VSANIPAIVL TGGPMLNGKL NGRTLGACTD CYQFTLEHKA
GNITDEQLTV AENAICRSDG HCMVMGTAST MAAIAEALGM ALPGCAAIPA PDSRRRHMAE
LTGKQIVQLV HRDIRPRDII TPESIDNAIR VTMACAGSTN AIIHLVAIAG RLGYRLPLER
FDEISATTPF IVNVRPSGKY QMEEFFEAGG VPSLMKEIEP LLHGGCLTVT GGTVTDNLQG
VLVPDRELIY PLAAPIAPQG GIAVLRGNLS PNGALIKQTA VSPHLRKHTG RAVVFTSPAD
LNARIDDPDL DVDENSVLVL QNAGPKGAPA MPEIGQIPIP KKLLLRGVRD MVRISDARIS
GTSYGTLIVH VAPEAAIGGP LGLVRDGDLI ELDIDGRKLE LHVDEATLRE RSAQWQAPPP
AYDRGYGLLF LERVLQADEG CDFDFLLPPE LRTTK
//
