ID W6TRN4_9SPHI Unreviewed; 570 AA.
AC W6TRN4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Dihydroxy-acid dehydratase {ECO:0008006|Google:ProtNLM};
GN ORFNames=N824_25545 {ECO:0000313|EMBL:ETZ22297.1};
OS Pedobacter sp. V48.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=509635 {ECO:0000313|EMBL:ETZ22297.1, ECO:0000313|Proteomes:UP000019145};
RN [1] {ECO:0000313|EMBL:ETZ22297.1, ECO:0000313|Proteomes:UP000019145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V48 {ECO:0000313|EMBL:ETZ22297.1,
RC ECO:0000313|Proteomes:UP000019145};
RX PubMed=24578271;
RA Bitzer A.S., Garbeva P., Silby M.W.;
RT "Draft Genome Sequence of Pedobacter sp. Strain V48, Isolated from a
RT Coastal Sand Dune in the Netherlands.";
RL Genome Announc. 2:e00094-e00014(2014).
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:ETZ22297.1}.
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DR EMBL; AWRU01000013; ETZ22297.1; -; Genomic_DNA.
DR RefSeq; WP_048905726.1; NZ_AWRU01000013.1.
DR AlphaFoldDB; W6TRN4; -.
DR STRING; 509635.N824_25545; -.
DR PATRIC; fig|509635.5.peg.2820; -.
DR eggNOG; COG0129; Bacteria.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000019145; Unassembled WGS sequence.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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 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}.
SQ SEQUENCE 570 AA; 61634 MW; D76577BE74F989DB CRC64;
MEKKLRSQQW FGKKGKDGFI YRAWMKNQGI PADEFQGKPV IGICNTWSEL TPCNAHFREL
AESVKRGVIE AGGFPVEFPV MSLGETLIKP TAMLYRNLVS MDVEESIRAN PIDGVVLMCG
CDKTTPALVM GACSVDIPSI VVSGGAMLTG KFQGKNIGTS DIWRFSESVR SGIMTEEELN
LAEAGMCRSR GHCAVMGTAS SMACMVESLG LSLPGNAAIP AADASRKVLA QFSGRRIVDM
VREDLKPSDV LVPKAFENAI KVNAAIGGST NFVIHLLAIA GRVGIELTID DFDKHSAGIP
LIANLQPSGE HFMEDLYYAG GLPAVMKEMQ RFLNAECITV NGRNIGQNLE RAQTLNQEVI
ASVESPFKLD SGVAVLKGNL CPEGAIIKPS AANPRLMQHT GRAVVFENIE DYKLRIDDPE
LVVDADSVLV LKNTGPKGYP GMPEVGNMGL PKKMLDLGVT DMVRISDGRM SGTGFGTVVL
HVSPETAENG TIALVKDGDM IELDVAGRRL SLLVPDEELD QRRALLADPV NQFKRGYARL
YVEHVEQAHL GADFDFLKGN SGSEVLRDSH
//
