ID   A0A2C6DM79_9GAMM        Unreviewed;       571 AA.
AC   A0A2C6DM79;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:PHI30327.1};
GN   ORFNames=CRN84_13775 {ECO:0000313|EMBL:PHI30327.1};
OS   Budvicia aquatica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Budviciaceae; Budvicia.
OX   NCBI_TaxID=82979 {ECO:0000313|EMBL:PHI30327.1, ECO:0000313|Proteomes:UP000224974};
RN   [1] {ECO:0000313|Proteomes:UP000224974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_387 {ECO:0000313|Proteomes:UP000224974};
RA   Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA   Sadzewicz L., Ott S., Zhao X., Nagaraj S., Vavikolanu K., Aluvathingal J.,
RA   Nadendla S., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (SEP-2017) 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:PHI30327.1}.
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DR   EMBL; PDDX01000001; PHI30327.1; -; Genomic_DNA.
DR   RefSeq; WP_029093575.1; NZ_PDDX01000001.1.
DR   AlphaFoldDB; A0A2C6DM79; -.
DR   STRING; 1111728.GCA_000427805_04142; -.
DR   OrthoDB; 9807077at2; -.
DR   Proteomes; UP000224974; Unassembled WGS sequence.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
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; 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   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224974}.
SQ   SEQUENCE   571 AA;  61959 MW;  E466122A10596834 CRC64;
     MQQKCQSARD LWSQLDALRL GMNYSKEDTK KPQVLIDDCY GESHPGSFHL GELGYETVLG
     VHESGGRAVR HHVTDICDGW GQGHDGMNYI LASREAIANM VEIHASVVPY DAGVLISSCD
     KSIPAHLIAA ARLDMPLLHI PGGSMRPAPN MSTSDLGGIT AKLKKGEISV KQVEAYQQCG
     CPTAGACQFM GTASTMQCMS EALGMALPGS ALIPATMSEI RRMARAAGHQ AMYLAEKNIT
     TGRILTPAAF ENAIKVHAAI GGSTNGLIHL PAIAHELGWE LKPEVFDRIN HQIPYLTNIQ
     PSGEYVTELM WFAGGIPMIQ WLLRDQLDLD VLTVTGRSLG DNLEMIQQSG FFERNHGYLA
     NYKVQPEDVI RKPESATKKG SIAILKGNIA PDGAVIKYAA CRADMHQHIG PAKVFNSEED
     AQQAIIHNQV EPGDVLFIRY EGPKGSGAPE MLMTTDAIVY DNRLDGRVAL ITDGRFSGAT
     SGPCVGHVSP EAADGGPIAL IEDGDVIEMN VPERKLNIIG VNGERKTEQE IDAIMAERKS
     RWVRPDYSAR RGIYKQFTER AASLMAGAYT S
//