ID C7QI36_CATAD Unreviewed; 580 AA.
AC C7QI36;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:ACU73081.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:ACU73081.1};
GN OrderedLocusNames=Caci_4217 {ECO:0000313|EMBL:ACU73081.1};
OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS B-24433 / ID139908).
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU73081.1, ECO:0000313|Proteomes:UP000000851};
RN [1] {ECO:0000313|EMBL:ACU73081.1, ECO:0000313|Proteomes:UP000000851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC {ECO:0000313|Proteomes:UP000000851};
RX PubMed=21304647; DOI=10.4056/sigs.17259;
RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT 139908).";
RL Stand. Genomic Sci. 1:119-125(2009).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; CP001700; ACU73081.1; -; Genomic_DNA.
DR AlphaFoldDB; C7QI36; -.
DR STRING; 479433.Caci_4217; -.
DR KEGG; cai:Caci_4217; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_3_1_11; -.
DR InParanoid; C7QI36; -.
DR Proteomes; UP000000851; 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: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, ECO:0000313|EMBL:ACU73081.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000851}.
SQ SEQUENCE 580 AA; 61845 MW; 166FE60D82EE1743 CRC64;
MAVSAPQLRS AAWFGEGATG GHLRAFSHRS RMRQLGYLPE EHLGKPVIAI LNTWSDINPC
HMHLRERAEQ VKRGVWQAGG FPLEFPVSTL SETFQKPTPM LYRNLLAMET EELLRSYPVD
GAVLMGGCDK TTPALLMGAA SAGFPALFVP AGPMLRGHHR GKTLGSGTDL FAYFDEYRAG
RVGECEMAEV EGGLARSPGH CMTMGTASTM TACAEALGMA LPGASSIPAV DSAHHRMAAA
SGMRAVAIAL EGVTPQQVMT REAFEDAAAT VLTLSGSTNA LIHLIAMAGR LGVELRLDDF
DAIGERVPVL ADVRPVGRFL MEDFYYAGGL RALLRELSEV PGVLHPDRPT VAGVPFGEYY
ADSQTHDPEV IRTPANPVAD HGGVAVLRGN LAPNGAVIKH LAAEPHLLTH SGPAVVFDSY
ADLQARIDDE SLAITEDTVL VLRGAGPLGG PGMPEYGMLP IPAYLLKQGV KDMVRISDAR
MSGTSYGTCV LHIAPESHAG GPLALVRTGD TITLDVPART LHLEVDDTEL ARRQAAWQPP
APPFERGYGS LYAAHITQAD QGCDFDFLAR PGTNPLPDPH
//
