ID   A0A1R1BXW2_9BACL        Unreviewed;       657 AA.
AC   A0A1R1BXW2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Dehydratase {ECO:0000313|EMBL:OMF14723.1};
GN   ORFNames=BK127_18630 {ECO:0000313|EMBL:OMF14723.1};
OS   Paenibacillus sp. FSL H7-0331.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1920421 {ECO:0000313|EMBL:OMF14723.1, ECO:0000313|Proteomes:UP000187480};
RN   [1] {ECO:0000313|EMBL:OMF14723.1, ECO:0000313|Proteomes:UP000187480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H7-0331 {ECO:0000313|EMBL:OMF14723.1,
RC   ECO:0000313|Proteomes:UP000187480};
RA   Beno S.M.;
RT   "Paenibacillus species isolates.";
RL   Submitted (NOV-2016) 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:OMF14723.1}.
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DR   EMBL; MRTH01000011; OMF14723.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R1BXW2; -.
DR   STRING; 1920421.BK127_18630; -.
DR   Proteomes; UP000187480; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050401; F:xylonate dehydratase 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; IPR017798; Dehydratase_YjhG/YagF.
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   NCBIfam; TIGR03432; yjhG_yagF; 1.
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:UP000187480}.
SQ   SEQUENCE   657 AA;  69540 MW;  EE97BA0EF4D2DED5 CRC64;
     MSEQLNQIMG TDHSQIYEIH THASGPEGSL PLTREMLLNS PSGDLFGLSQ NVGMGWKPSR
     LSGKQFLLLS TQGGIRKDDG TPVALGYHTG HWEIGLLMEE AANEIADNGG LPFAGYVSDP
     CDGRSQGTTG MFDSLPYRND AAIVFRRLVR SLPTRRGVIG VATCDKGLPA MMMALAGIHD
     LPCIIVPGGV TLPPTNGEDA GKIQTIGARY SNGELSLEDA ADLGCRACAT PGGGCQFLGT
     AATAQVVAEA LGMTIPHAAL SPSGQPIWKE MSRQSARAMM AMEAKGIKMK DILTESAIRN
     AMAVHAAFGG STNLLLHIPA IAHAAGLPVP TVQDWIKINK SVPRLVSVLP NGPDYHPTVR
     VFLAGGVPEV MLHLRRLGVL DVDVMTVTGE KLSTVLDWWE TSERRKALKK LLLDADGVEA
     DAVIMTPEQS KRRGLTSTVT FPMGNLAPEG SVIKSTAIDA SVVGEDGVYR HRGQAKVYTS
     EREAIFAIKS GGVVAGDIMV LIGRGPSGTG MEETYQLTSA LKHLPFGKYV SLITDARFSG
     VSTGACIGHV GPEALAGGPI GKLRNGDTID IVVNRDTLEG SVHFIGHGDD LVSPEEGALI
     LQARDPHPDL APDAKLPDDT RLWAALQAVS GGTWRGSIYD VERIVTALEA GKKSLGW
//