ID A0A270B9N0_9SPHN Unreviewed; 598 AA.
AC A0A270B9N0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:PAL21737.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:PAL21737.1};
GN ORFNames=CD928_15425 {ECO:0000313|EMBL:PAL21737.1};
OS Sphingopyxis sp. GW247-27LB.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=2012632 {ECO:0000313|EMBL:PAL21737.1, ECO:0000313|Proteomes:UP000216381};
RN [1] {ECO:0000313|Proteomes:UP000216381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW247-27LB {ECO:0000313|Proteomes:UP000216381};
RA Ray J., Price M.N., Deutschbauer A.M.;
RL Submitted (JUN-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:PAL21737.1}.
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DR EMBL; NIWD01000009; PAL21737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A270B9N0; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000216381; Unassembled WGS sequence.
DR GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:PAL21737.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ SEQUENCE 598 AA; 63793 MW; 3B51B558C71E1575 CRC64;
MSVSHPPMLR SRAWFDNPDN VDMTALYLER YLNFGLSLEE LQSGKPIIGI AQTGSDLSPC
NRHHLVLAER VREGIREAGG IAIEFPVHPI QETGKRPTAG LDRNLAYLSL VETLYGYPLD
GVVLTVGCDK TAPACLMAAA TVNIPAIALS VGPMLNGWHK GERTGSGTIV WKARQMLAAG
EIDDAEFIRL VASSAPSTGY CNTMGTATTM NSLTEALGMS LPGSAAIPAP YRDRQEVAYR
TGKRAVEMVR EDLKPSDIMT RDAFLNAIAV SSAIGGSTNA PIHLAAIARH IGVDLPLKTW
QDHGHAIPLL VNLQPAGEYL GEDYYRAGGV PAVVAQLMGQ GLIAEEAMTA NGRTIGENCR
AVEIEDEKVI RRYADPLKAD AGFIVLSGNL FDSAIMKTSV ISDEFRARYL SNPDDPDAFE
GPVAVFDGPE DYHRRIDDPA TGITAETLLV MRGAGPIGYP GAAEVVNMRP PAHLILDGVH
ALPCLGDGRQ SGTSGSPSIL NASPEAAAGG ALALLRTGDR VRIDLRRATA NVLVEAAELD
ARRQALEAEG GYAYPASQTP WQELQRSVVG QLGTGAILEG AEAYQRIAQT RGLPRDNH
//