ID Q1QYG0_CHRSD Unreviewed; 581 AA.
AC Q1QYG0;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=L-arabinonate dehydratase {ECO:0000313|EMBL:ABE58498.1};
DE EC=4.2.1.25 {ECO:0000313|EMBL:ABE58498.1};
GN OrderedLocusNames=Csal_1142 {ECO:0000313|EMBL:ABE58498.1};
OS Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS NCIMB 13768 / 1H11).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=290398 {ECO:0000313|EMBL:ABE58498.1, ECO:0000313|Proteomes:UP000000239};
RN [1] {ECO:0000313|EMBL:ABE58498.1, ECO:0000313|Proteomes:UP000000239}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11
RC {ECO:0000313|Proteomes:UP000000239};
RX PubMed=22675587; DOI=10.4056/sigs.2285059;
RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT "Complete genome sequence of the halophilic and highly halotolerant
RT Chromohalobacter salexigens type strain (1H11(T)).";
RL Stand. Genomic Sci. 5:379-388(2011).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; CP000285; ABE58498.1; -; Genomic_DNA.
DR RefSeq; WP_011506444.1; NC_007963.1.
DR AlphaFoldDB; Q1QYG0; -.
DR STRING; 290398.Csal_1142; -.
DR KEGG; csa:Csal_1142; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_3_1_6; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000000239; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050020; F:L-arabinonate dehydratase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:ABE58498.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000239}.
SQ SEQUENCE 581 AA; 62493 MW; 1389A943AFD57E3D CRC64;
MTHKKRPLRS AEWFGNDDKN GFMYRSWMKN QGIPDHEFRG KPIIGICNTF SELTPCNAHF
RKLAEHVKKG VLEAGGYPVE FPVFSNGESN LRPTAMFTRN LASMDVEEAI RGNPLDAVVL
LVGCDKTTPA LLMGAASCDI PTIVVTGGPM LNGKHKGRDI GSGTVVWQLS EEVKAGKISL
HDFMAAEAGM SRSAGTCNTM GTASTMACMA ESLGTSLPHN AAIPAVDSRR YVLAHLSGNR
IVEMVDEDLT LSKVLTKSAF ENAIRTNAAI GGSTNAVIHL QAIAGRMGVD LTLDDWTRVG
RGTPTIVDLQ PSGRYLMEEF YYAGGLPAVL RRLGEADRLP HKDALTVNGK TLWENVQDAP
LYNDAVILPL DAPLREDGGM CVMRGNLAPN GAVLKPSAAT PALMQHRGRA VVFENFDDYK
ARINDPDLDV TADDILVMKN CGPRGYHGMA EVGNMGLPAK LLEQGVTDMV RISDARMSGT
AYGTVVLHVA PEAAAGGPLA AVRNGDWIAL DAYSGKLHLE VDDAEIASRL AEADPTAEST
RIASTGGYRQ LYIEHVLQAD QGCDFDFLVG CRGAEVPRHS H
//
