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
//