ID A0A2R8APL2_9RHOB Unreviewed; 593 AA.
AC A0A2R8APL2;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=L-arabonate dehydratase {ECO:0000313|EMBL:SPF78018.1};
DE EC=4.2.1.25 {ECO:0000313|EMBL:SPF78018.1};
GN Name=araC_1 {ECO:0000313|EMBL:SPF78018.1};
GN ORFNames=PRI8871_00607 {ECO:0000313|EMBL:SPF78018.1};
OS Pseudoprimorskyibacter insulae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudoprimorskyibacter.
OX NCBI_TaxID=1695997 {ECO:0000313|EMBL:SPF78018.1, ECO:0000313|Proteomes:UP000244904};
RN [1] {ECO:0000313|Proteomes:UP000244904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8871 {ECO:0000313|Proteomes:UP000244904};
RA Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; OMOJ01000001; SPF78018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8APL2; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000244904; Unassembled WGS sequence.
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:SPF78018.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000244904}.
SQ SEQUENCE 593 AA; 64398 MW; 3273F83B38EC6331 CRC64;
MSDTRANKRF RSQEWFDNPN NPGMTALYVE RYQNQEYTRD ELQGGKPVIG IANTGSDLAP
CNKIHVFLMD RIKAGIRAAG GIPMEFPVHP IQETGKRPTA ALDRNLSYLG LVEVLHGYPI
DGVVLTTGCD KTTPAMLMGA ATADLPAIAL NGGPMLDGWW KGKRAGSGTI IWESRRLLAE
EKIDYEEFMS RVCSSAPSLG HCNTMGTAST MNAMAEALGM SLTGNSAIPA PFRERMAMAY
ETGKRIVEMV YEDLKPSDIL TREAFENAIV VNAAIGGSTN APPHLQAIAR HAGVELNVKD
WETVGYDVPL LLNMQPAGEF LGESFFRAGG VPAVMEELRK AGRIHEGAMT ATGKTMGENV
TGKGTEDEAV IKTYDKPMRV NAGFKVLSGN LFDSALMKTS VISADFQKRF LSKPGMEGVH
EARAIVFEGP EDYHDRINDP SLNIDEHCIL FIRNVGCVGY PGSAEVVNMQ PPDALIRQGI
NHLPTVGDGR QSGTSESPSI LNASPESVVG GGLAYLKTGD TVRLDLNAST MNALVDDAEW
QARIDAWEAP EIRSQTPWQE IYRTHVGQLS DGGCLELATA YQKVAKDLPR DNH
//