ID A0A0U2KVC2_9BACL Unreviewed; 563 AA.
AC A0A0U2KVC2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:ALS20578.1};
GN ORFNames=IJ22_01860 {ECO:0000313|EMBL:ALS20578.1};
OS Paenibacillus naphthalenovorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=162209 {ECO:0000313|EMBL:ALS20578.1, ECO:0000313|Proteomes:UP000061660};
RN [1] {ECO:0000313|Proteomes:UP000061660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-Y {ECO:0000313|Proteomes:UP000061660};
RA Butler R.III., Wang J., Stark B.C., Pombert J.-F.;
RT "Complete genome sequences of two moderately thermophilic Paenibacillus
RT species.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALS20578.1, ECO:0000313|Proteomes:UP000061660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=32O-Y {ECO:0000313|EMBL:ALS20578.1,
RC ECO:0000313|Proteomes:UP000061660};
RX PubMed=26868401;
RA Butler R.R.III., Wang J., Stark B.C., Pombert J.F.;
RT "Complete Genome Sequences of Two Interactive Moderate Thermophiles,
RT Paenibacillus napthalenovorans 32O-Y and Paenibacillus sp. 32O-W.";
RL Genome Announc. 4:e01717-15(2016).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; CP013652; ALS20578.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U2KVC2; -.
DR STRING; 162209.IJ22_01860; -.
DR KEGG; pnp:IJ22_01860; -.
DR PATRIC; fig|162209.4.peg.190; -.
DR Proteomes; UP000061660; Chromosome.
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:UP000061660}.
SQ SEQUENCE 563 AA; 61273 MW; AA5D7028DD8AA326 CRC64;
MKTNTSYGDS GFSHFIRMAF QRHLGYDEQD FDKPVIGICN TFSEINRCHS HIQPMVDAIK
QGVIMAGGIP LEFPTISIGE MFTSPTTMLY RNLAAMDTEE MITAQPIDGV VLIGGCDKMT
PAQLMGAASA NKPAIMFTGG PMNNGEYNGK TLGACSDCRF FWQEYKAGTV SEEEINEINA
QLAPTAGHCM VMGSASTMAA CSEALGMMLP GGAAAPATVH ERMRLAKETG KAIVRLVQEH
IRPSDIMTEK AFDNAIRTLM AVGGSSNAVI HLIAIARRLG IGLTLDRFEA LSQTTPFIAN
LRPAGEYQMQ DFYYAGGVPA VLKELSPLLH LDELTVTGKT LKDNLKDVQS KPHYSHIIKS
LKAPLYPNGG IAVLRGNLAP DGAIIKPKAV IDKKLLKHKG QAVVFTSIED MEQRIHDPDL
EVTPDSILVL QHAGPVGAPG MPEAGMLPIP QKLLKQGVRD MLRLSDCRMS GTAFGTVVLH
IAPEAAVGGP IGLVKDGDWI ELDAERGSLE LLVSEEELTR RKESWSPPQF TDTGYKWLYR
RHVLQADQGC DFDFHFPRER VGG
//