ID Q2IV17_RHOP2 Unreviewed; 569 AA.
AC Q2IV17;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Dihydroxyacid dehydratase {ECO:0000313|EMBL:ABD07943.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:ABD07943.1};
GN OrderedLocusNames=RPB_3247 {ECO:0000313|EMBL:ABD07943.1};
OS Rhodopseudomonas palustris (strain HaA2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316058 {ECO:0000313|EMBL:ABD07943.1, ECO:0000313|Proteomes:UP000008809};
RN [1] {ECO:0000313|EMBL:ABD07943.1, ECO:0000313|Proteomes:UP000008809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HaA2 {ECO:0000313|EMBL:ABD07943.1,
RC ECO:0000313|Proteomes:UP000008809};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL Submitted (JAN-2006) 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; CP000250; ABD07943.1; -; Genomic_DNA.
DR RefSeq; WP_011442127.1; NC_007778.1.
DR AlphaFoldDB; Q2IV17; -.
DR STRING; 316058.RPB_3247; -.
DR KEGG; rpb:RPB_3247; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_3_0_5; -.
DR OrthoDB; 7793094at2; -.
DR Proteomes; UP000008809; Chromosome.
DR GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:ABD07943.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ SEQUENCE 569 AA; 60470 MW; DAF1176120D94AB9 CRC64;
MADGLRKGLT SYGDAGFSLF LRKAFIKAMG YSDDALERPI VGITNTHSDY NPCHGNVPQI
IEAVKRGVML AGAMPMVFPT ISIAESFAHP TSMYLRNLMA MDTEEMIRAQ PMDAVVVIGG
CDKTLPAQIM AAVSADLPTV VIPVGPMVVG HHKGEVLGAC TDCRRLWAKH RAGEIDEAEI
EAVNGRLAPS VGTCMVMGTA STMACLTEAM GLSLPMSATI PAPHAERFRS AEESGRVAAA
MAKAKGPKPS DLLTPAAFRN AQVVLQAIGG STNGLIHLTA IAGRVPHKID LDGFDRIGRD
VPVLVDLKPS GDHYMEHFHH AGGVPKLMAQ LGELIDLDAR TITGAPLRDI VARAEHVQGQ
DVIRSRDNPI RREGGLAMLT GNLAPRGAVI KHAAASPQLM QHTGRAVVFD SVEDMTLRID
DPDLDVAADD VLVLRNAGPR GAPGMPEAGY LPIPMKLARA GIKDMVRISD ARMSGTAFGT
IVLHITPESA DGGPLALVET GDRIALDVAA RRIDLLVDES ELARRRAALS SSAAARPTRG
YAQLFHDTIL QADEGCDFDF LTAAGRSER
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