ID A0A0A1VIC1_9BURK Unreviewed; 575 AA.
AC A0A0A1VIC1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Dihydroxyacid dehydratase/phosphogluconate dehydratase {ECO:0000313|EMBL:GAD23032.1};
GN ORFNames=AVS7_02792 {ECO:0000313|EMBL:GAD23032.1};
OS Acidovorax sp. MR-S7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1268622 {ECO:0000313|EMBL:GAD23032.1};
RN [1] {ECO:0000313|EMBL:GAD23032.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-S7 {ECO:0000313|EMBL:GAD23032.1};
RX DOI=10.1128/genomeA.00412-13;
RA Miura T., Kusada H., Kamagata Y., Hanada S., Kimura N.;
RT "Genome Sequence of the Multiple-beta-Lactam-Antibiotic-Resistant Bacterium
RT Acidovorax sp. Strain MR-S7.";
RL Genome Announc. 1:e00412-13(2013).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; DF238933; GAD23032.1; -; Genomic_DNA.
DR RefSeq; WP_020228943.1; NZ_DF238933.1.
DR AlphaFoldDB; A0A0A1VIC1; -.
DR STRING; 1268622.AVS7_02792; -.
DR eggNOG; COG0129; Bacteria.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000030646; 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:SF2; DIHYDROXY-ACID DEHYDRATASE; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030646}.
SQ SEQUENCE 575 AA; 62701 MW; 8B7C349C1697F518 CRC64;
MKRTYETLRS ARWFAPDDFR SFGHRSRVLQ MGYGYEDWVG KPVIAIVNTW SDANQCHAHF
KQRVEDVKRG VLQAGGFPLE LPAISLSESM VKPTTMLYRN FLAMETEELM RSHPVDGAVL
MGGCDKTTPG LTMGALSMGI PFIYLPAGPM LRGNWKGQVL GSGSDAFKYW DERRAGRLSD
QAWNEMEAGI ARSHGTCMTM GTAATMMGIA EAVGLALPGA SSIPAADANH IRMSAECGRR
IVEMVWDDFT PAKMLTRANF ENGIACAMAM GCSTNAIIHL IAMSRRAGHP VSLQDFDAFS
RHVPVIANIR PSGDAYLMED FFYAGGLRAM LERIRCHLKT EALTVNGRTI GENIAGSEVY
HDDVIRPLSN PIYAEGALAV LKGNLAPDGV VIKPSACAPH LLQHTGRALV FDDYPSLKKA
VEDPDLDVTG DDVLVLRNAG PLGAGMPEWG MLPIPTKLLK QGVKDMLRLS DARMSGTSYG
GCLLHCAPEA AIGGPLALVK TGDRITVDVP ARSIHLEVSD EELAARSKAW KPAPPRYERG
YGWMFGRHIK QADEGCDFDF LETTFGTPVP EPDIF
//
