ID A0A099RU13_9CLOT Unreviewed; 574 AA.
AC A0A099RU13;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:KGK83834.1};
GN ORFNames=DP68_17100 {ECO:0000313|EMBL:KGK83834.1};
OS Clostridium sp. HMP27.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1487921 {ECO:0000313|EMBL:KGK83834.1, ECO:0000313|Proteomes:UP000030009};
RN [1] {ECO:0000313|EMBL:KGK83834.1, ECO:0000313|Proteomes:UP000030009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMP27 {ECO:0000313|EMBL:KGK83834.1,
RC ECO:0000313|Proteomes:UP000030009};
RA Tan B.F., Foght J., Budwill K.;
RT "Draft genome sequence of Clostridium sp. HMP27 isolated from a coal
RT degrading methanogenic culture.";
RL Submitted (APR-2014) 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:KGK83834.1}.
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DR EMBL; JMFY01000045; KGK83834.1; -; Genomic_DNA.
DR RefSeq; WP_035311633.1; NZ_JMFY01000045.1.
DR AlphaFoldDB; A0A099RU13; -.
DR STRING; 1487921.DP68_17100; -.
DR eggNOG; COG0129; Bacteria.
DR Proteomes; UP000030009; 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: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; PTHR43661; D-XYLONATE DEHYDRATASE; 1.
DR PANTHER; PTHR43661:SF3; D-XYLONATE DEHYDRATASE YAGF-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.
DR PROSITE; PS00887; ILVD_EDD_2; 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:ARBA00022714};
KW Reference proteome {ECO:0000313|Proteomes:UP000030009}.
SQ SEQUENCE 574 AA; 62322 MW; 322195218FC2469C CRC64;
MSNIKQKSAP ERLLWAQFDA LQMGSGWDEE DITKPQILVE DVFGDSHPGS VHLNKLTDQA
KYGIFERGGF PAQFHATDIC DGCAQGHDGM NYILASREVL CDMVEIHASV SPWDGMILAA
SCDKSIPAHL KAAARLDIPT IFIPGGSMRP GPNMTTSLVA GDISLRQKRK GEITNQEIRD
YKLTGCPSVG ACTFLGTAST MQCMAEALGL ALPGSALMPA TMTDILRNAR KAGRIIMELV
EKGITASRIL TREAFINAII IHSAIGGSTN ATIHLPSIAL ELGIELEPEL FDEINHRIPH
IGNINPSGQH LTETFWFAGG IPMVQLILKD YLNLDVMTAT GKTLGENLED LQRENYFERN
LGYLHNYGVK REEVIFPVEN VKEIGSIAIL KGNIAPEGSV VKYSACAENM RFHKGTARVY
NCEEDAYNAV VNGDINPGDV IVVRYEGPRG SGMPEMLMTT EAIVCDKRLN GTVSLITDGR
FSGATRGAAI GHVSPEAASG GPLAWVVTGD IIEYNIEKRA LNVVGINGVE MPLKEVDRVF
AERAREGIIP RPPRKGIFKR YTDSALSAMK GAGY
//
