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Database: UniProt
Entry: J3AF72_9CAUL
LinkDB: J3AF72_9CAUL
Original site: J3AF72_9CAUL 
ID   J3AF72_9CAUL            Unreviewed;       578 AA.
AC   J3AF72;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Dihydroxyacid dehydratase/phosphogluconate dehydratase {ECO:0000313|EMBL:EJL30319.1};
GN   ORFNames=PMI01_03179 {ECO:0000313|EMBL:EJL30319.1};
OS   Caulobacter sp. AP07.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=1144304 {ECO:0000313|EMBL:EJL30319.1, ECO:0000313|Proteomes:UP000007300};
RN   [1] {ECO:0000313|EMBL:EJL30319.1, ECO:0000313|Proteomes:UP000007300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP07 {ECO:0000313|EMBL:EJL30319.1,
RC   ECO:0000313|Proteomes:UP000007300};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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:EJL30319.1}.
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DR   EMBL; AKKF01000173; EJL30319.1; -; Genomic_DNA.
DR   RefSeq; WP_007670508.1; NZ_AKKF01000173.1.
DR   AlphaFoldDB; J3AF72; -.
DR   PATRIC; fig|1144304.3.peg.3028; -.
DR   Proteomes; UP000007300; Unassembled WGS sequence.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ   SEQUENCE   578 AA;  61530 MW;  A0B393EE1D250E52 CRC64;
     MGQGNGGGRF RSSGSYGKLD RDGFIHRSWM KSQGLPDNVF DGRPVIGICN TWSEITPCNA
     GLRDIAEHVK RGVWEAGGLP LEFPAISLGE TQMRPTAMLF RNLLAMDVEE SIRGNPIDGV
     VLLGGCDKTT PGQMMGAASV DLPTIVISSG PMLNGKFRGK DIGSGTDVWK FSEAVRAGEM
     TLPDFMSAES GMSRSPGTCM TMGTASTMAS IVEAMGMSLP YNASIPAVDA RRKAMSHETG
     RTIVRMVHDG RTMSQVATRA AFENALRVHA AIGGSTNAVV HLLALAGRLG VELTLEDFDN
     LSRDVPLLVD LQPSGRFLME DLHYAGGVPA VMKQLEPFLD PTALTVTGAP IGAQYAQAEV
     YNAEVIRTVE NPVKPDSGIW VLRGNLAPGG AVMKPSAASP ELLSHKGKAV VFETIEDFKA
     RIDDPDLDVD AGSILVLKGC GPKGYPGMPE VGNMPLPTKL LEKGVKDMVR ISDARMSGTA
     FGTVILHVSP EADAGGPLAI VRNGDEIVLD GPSRSLSLLI SDEEMATRLA HWRENQPPPK
     ATRGYAKLYI DHVLQADKGC DLDFLVGSSG SVVTRESH
//
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