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Database: UniProt
Entry: J3Z109_CARRU
LinkDB: J3Z109_CARRU
Original site: J3Z109_CARRU 
ID   J3Z109_CARRU            Unreviewed;       547 AA.
AC   J3Z109;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   03-MAY-2023, entry version 43.
DE   SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:AFP83884.1};
GN   Name=ilvD {ECO:0000313|EMBL:AFP83884.1};
GN   ORFNames=A353_030 {ECO:0000313|EMBL:AFP83884.1};
OS   Candidatus Carsonella ruddii HC isolate Thao2000.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Zymobacter group; Candidatus Carsonella.
OX   NCBI_TaxID=1202538 {ECO:0000313|EMBL:AFP83884.1, ECO:0000313|Proteomes:UP000003934};
RN   [1] {ECO:0000313|EMBL:AFP83884.1, ECO:0000313|Proteomes:UP000003934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HC {ECO:0000313|EMBL:AFP83884.1,
RC   ECO:0000313|Proteomes:UP000003934};
RX   PubMed=22821013; DOI=10.1093/molbev/mss180;
RA   Sloan D.B., Moran N.A.;
RT   "Genome reduction and co-evolution between the primary and secondary
RT   bacterial symbionts of psyllids.";
RL   Mol. Biol. Evol. 29:3781-3792(2012).
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC       {ECO:0000256|ARBA:ARBA00006486}.
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DR   EMBL; CP003543; AFP83884.1; -; Genomic_DNA.
DR   AlphaFoldDB; J3Z109; -.
DR   STRING; 1202538.A353_030; -.
DR   KEGG; crh:A353_030; -.
DR   PATRIC; fig|1202538.3.peg.29; -.
DR   HOGENOM; CLU_014271_4_1_6; -.
DR   OrthoDB; 9807077at2; -.
DR   Proteomes; UP000003934; Chromosome.
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; PTHR21000; DIHYDROXY-ACID DEHYDRATASE DAD; 1.
DR   PANTHER; PTHR21000:SF5; DIHYDROXY-ACID DEHYDRATASE, MITOCHONDRIAL; 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:UP000003934}.
SQ   SEQUENCE   547 AA;  60396 MW;  4825FB9D0DBB4640 CRC64;
     MKSNLITKWP ERAANRAMLR AVGYKSNDFL KYQVGIASTW SNITPCNNHI NILSKATEYG
     VNKYCKGTIF NTITVSDGIS NGNLGMKYSL LSREIISSSI ETVCNAQNFD SIISIGGCDK
     NIPGCILGMC KLNLPSIFIY SGTILPGKNR TDIISVFESL GKYYSKKINE NQLLNIEKNS
     IIGSGSCSGM YTANSMAIAS EIIGISLPNS SLQNAQSINK IINCINSGKI IFNLLKKNIK
     IKDIITYKSI LNAIKVISLL GGSTNCILHL LSIANSLNIK ISLYDIKSIT NNLPTISDLK
     PSGIFFISDL INCGGIQKFL KFLLEIKLLD GDCLTITGNS LKENLKNIKN NYVNKILKNI
     NFPLKKTNQI KILFGNLSKN GCISKISGKE GEIFFGKSKI FNSEEESIEY IYKKKIYKKT
     IIVIRFEGPK GGPGMREMLT PTSALIGIGV KKDIALITDG RFSGGSHGFV VGHISPEAYN
     KGEISILKEN DILMIDTINN NIIFFVNNNN INNRKKFFFN YSKISFGILN LYRKNSLDSS
     KGASFDY
//
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