(data stored in ACNUC1104 zone)

SWISSPROT: D3VHV9_XENNA

ID   D3VHV9_XENNA            Unreviewed;       616 AA.
AC   D3VHV9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 55.
DE   RecName: Full=Dihydroxy-acid dehydratase {ECO:0000256|HAMAP-Rule:MF_00012, ECO:0000256|SAAS:SAAS00943824};
DE            Short=DAD {ECO:0000256|HAMAP-Rule:MF_00012};
DE            EC=4.2.1.9 {ECO:0000256|HAMAP-Rule:MF_00012, ECO:0000256|SAAS:SAAS00943824};
GN   Name=ilvD {ECO:0000256|HAMAP-Rule:MF_00012,
GN   ECO:0000313|EMBL:CBJ88448.1};
GN   OrderedLocusNames=XNC1_0371 {ECO:0000313|EMBL:CBJ88448.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88448.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88448.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate
CC         + H2O; Xref=Rhea:RHEA:20936, ChEBI:CHEBI:11424,
CC         ChEBI:CHEBI:11851, ChEBI:CHEBI:15377; EC=4.2.1.9;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00012,
CC         ECO:0000256|SAAS:SAAS01115286};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00012};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_00012};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 3/4. {ECO:0000256|HAMAP-
CC       Rule:MF_00012, ECO:0000256|SAAS:SAAS00943826}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC       from pyruvate: step 3/4. {ECO:0000256|HAMAP-Rule:MF_00012,
CC       ECO:0000256|SAAS:SAAS00943830}.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000256|HAMAP-
CC       Rule:MF_00012, ECO:0000256|SAAS:SAAS00943829}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; FN667742; CBJ88448.1; -; Genomic_DNA.
DR   RefSeq; WP_010845338.1; NC_014228.1.
DR   STRING; 406817.XNC1_0371; -.
DR   EnsemblBacteria; CBJ88448; CBJ88448; XNC1_0371.
DR   KEGG; xne:XNC1_0371; -.
DR   eggNOG; ENOG4105C01; Bacteria.
DR   eggNOG; COG0129; LUCA.
DR   HOGENOM; HOG000173155; -.
DR   KO; K01687; -.
DR   OMA; IPGHVHL; -.
DR   UniPathway; UPA00047; UER00057.
DR   UniPathway; UPA00049; UER00061.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.30.80; -; 1.
DR   HAMAP; MF_00012; IlvD; 1.
DR   InterPro; IPR042096; Dihydro-acid_dehy_C.
DR   InterPro; IPR004404; DihydroxyA_deHydtase.
DR   InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR   InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR   InterPro; IPR037237; IlvD/EDD_N.
DR   Pfam; PF00920; ILVD_EDD; 1.
DR   SUPFAM; SSF143975; SSF143975; 1.
DR   TIGRFAMs; TIGR00110; ilvD; 1.
DR   PROSITE; PS00886; ILVD_EDD_1; 1.
DR   PROSITE; PS00887; ILVD_EDD_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VHV9.
DR   SWISS-2DPAGE; D3VHV9.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00012,
KW   ECO:0000256|SAAS:SAAS00943818};
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00012,
KW   ECO:0000256|SAAS:SAAS00943821};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
KW   Rule:MF_00012, ECO:0000256|SAAS:SAAS00943815};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00012, ECO:0000256|SAAS:SAAS00943817};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00012,
KW   ECO:0000256|SAAS:SAAS00943822};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00012, ECO:0000256|SAAS:SAAS00943827,
KW   ECO:0000313|EMBL:CBJ88448.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00012,
KW   ECO:0000256|SAAS:SAAS00943828};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075}.
FT   METAL       122    122       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00012}.
FT   METAL       195    195       Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP-
FT                                Rule:MF_00012}.
SQ   SEQUENCE   616 AA;  65780 MW;  5210CC8F9A297CEE CRC64;
     MPKYRSATTT HGRNMAGARA LWRATGMTDA DFGKPIIAVV NSFTQFVPGH VHLRDLGKLV
     AEQIEASGGV AKEFNTIAVD DGIAMGHGGM LYSLPSRELI ADSVEYMVNA HCADAMVCIS
     NCDKITPGML MASLRLNIPV IFVSGGPMEA GKTRLSDQII KLDLVDAMIQ GANPNVSDEQ
     SDQIERSACP TCGSCSGMFT ANSMNCLTEA LGLSQPGNGS LLATHADRKT LFINAGKRIV
     ALTKRYYEKN DDSALPRNIA TKAAFENAMT LDIAMGGSTN TVLHLLAAAQ EGEVDFTMAD
     IDRLSRQVPH LCKVAPSTQK YHMEDVHRAG GVMGILGELD RAGLLRRGVK NILGLDLAQT
     LVQYDIMLTE NEHVKHMYSA GPAGIRTTQA FSQDCRWPSL DIDRQEGCIR ERAYAYSQDG
     GLAVLFGNVA ANGCIVKTAG VDEGSLTFRG PAKVYESQDD AVDAILGGKV VAGDVVIIRY
     EGPKGGPGMQ EMLYPTTYLK SMGLGKSCAL ITDGRFSGGT SGLSIGHVSP EAANGGLIGL
     IQDGDIIEID IPNRKIQLDV AETELAERAQ AELSRGDKAW TPKSRERQVS FALRAYASLA
     TSADKGAVRD KTKLGC
//

If you have problems or comments...

PBIL Back to PBIL home page