ID B6EP03_ALISL Unreviewed; 490 AA.
AC B6EP03;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:CAQ77738.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:CAQ77738.1};
GN Name=ilvD {ECO:0000313|EMBL:CAQ77738.1};
GN OrderedLocusNames=VSAL_I0053 {ECO:0000313|EMBL:CAQ77738.1};
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=316275 {ECO:0000313|EMBL:CAQ77738.1, ECO:0000313|Proteomes:UP000001730};
RN [1] {ECO:0000313|EMBL:CAQ77738.1, ECO:0000313|Proteomes:UP000001730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238 {ECO:0000313|EMBL:CAQ77738.1,
RC ECO:0000313|Proteomes:UP000001730};
RX PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT LFI1238 shows extensive evidence of gene decay.";
RL BMC Genomics 9:616-616(2008).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; FM178379; CAQ77738.1; -; Genomic_DNA.
DR RefSeq; WP_012548958.1; NC_011312.1.
DR AlphaFoldDB; B6EP03; -.
DR KEGG; vsa:VSAL_I0053; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_4_2_6; -.
DR Proteomes; UP000001730; Chromosome 1.
DR GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:UniProtKB-EC.
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; 2.
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, ECO:0000313|EMBL:CAQ77738.1}.
SQ SEQUENCE 490 AA; 51704 MW; F104E5AE1F0F2565 CRC64;
MSTTPKNRYR SATTTHGRNM AGARALWRAT GVKEEDFGKP IIAVVNSFTQ FVPGHVHLKD
MGQLVAGEIE KAGGIAKEFN TIAVDDGIAM GHGGMLYSLP SRELIADSVE YMVNAHCADA
MVCISNCDKI TPGMMMAAMR LNIPVIFVSG GPMEAGKTKL SDQIIKLDLV DAMIQGADPT
VSDAQSEQIE RSACPTCGSC SGMFTANSMN CLTEALGLSQ PGNGSMLATH ADREELFINA
GKRIVTLTKR YYEQGDDSAL PRNIANKAAF ENAMALDIAM GGSSNTVLHL IASAQEGGLA
VLSGNIAVDG CIVKTAGVDE DNLKFQGPAI VFESQDTAVE NILAGEVKAG NVVVIRYEGP
KGGPGMQEML YPTTYLKSMG LGKACALLTD GRFSGGTSGL SIGHASPEAA SGGTIGLVKT
GDIITIDIPN RSITLDVPEA ELSERRAEQD KLGWKPVNRQ REVSFALKAY AMMATSADKG
AVRDRSKLEG
//
