ID C7JHS6_ACEP3 Unreviewed; 595 AA.
AC C7JHS6;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:BAH99530.1};
GN OrderedLocusNames=APA01_13840 {ECO:0000313|EMBL:BAH99530.1};
OS Acetobacter pasteurianus (strain NBRC 105184 / IFO 3283-01).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=634452 {ECO:0000313|EMBL:BAH99530.1, ECO:0000313|Proteomes:UP000000948};
RN [1] {ECO:0000313|EMBL:BAH99530.1, ECO:0000313|Proteomes:UP000000948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105184 / IFO 3283-01 {ECO:0000313|Proteomes:UP000000948};
RX PubMed=19638423; DOI=10.1093/nar/gkp612;
RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., Harada T.,
RA Hirakawa H., Kuhara S., Matsushita K., Fujita N., Shirai M.;
RT "Whole-genome analyses reveal genetic instability of Acetobacter
RT pasteurianus.";
RL Nucleic Acids Res. 37:5768-5783(2009).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; AP011121; BAH99530.1; -; Genomic_DNA.
DR AlphaFoldDB; C7JHS6; -.
DR STRING; 634452.APA01_13840; -.
DR KEGG; apt:APA01_13840; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_3_1_5; -.
DR Proteomes; UP000000948; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 275..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 64910 MW; 46042DA3AED9AE6B CRC64;
MRMTEDDRIS SAAVTPEQAG RRKLRSERWF GPADLRSFGH RSRAMQMGYD AKDWEGKPVI
AILNTWSDIN PCHMHFRQRV EDVKHGILEA GGFPMELPAI SLSENFMKPT TMLYRNMLAM
EAEELLRAYP ADGAVLMGGC DKTTPGLLLG AISMDIPAIY VPAGPMLRGN WHGKLLGSGA
DSWKYWDELR AGKITQEDWQ GVEEGIARSA GTCMTMGTAS TMTAIAEALG LSLPGASSIP
AVDSNHIRMA KSSGRRIVKM VWEDLKPSKI LTRAAFLNAI AVAMAMGCST NAIIHVIAMA
RRAGIDISLD DFDRSSRIVP VIANVRPTGT TYLMEDFYYA GGLAALIKRI SNFLDLSCLT
VTGKTIGENT ANAEVYNDDV IRPLDKPMFT GEAGGALTVL RGNIAPDGCV MKPACCDPKF
HKHSGPALVF DDYPSMKKAI DDENLDVTEN HVLVLRNAGP LGGPGMPEWG MLPIPKKLIK
QGVRDMLRLS DARMSGTSYG ACILHVAPEA YIGGPLALLK TGDIISVDVE ARSVSVEISE
EEMERRRKTW KAPPARYGRG YGWMAAHHIV QADKGCDFDF LQTDFGAPVS EPVIY
//
