ID A0A1A7RBZ5_9GAMM Unreviewed; 595 AA.
AC A0A1A7RBZ5;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:OBX28978.1};
GN ORFNames=A9J31_14545 {ECO:0000313|EMBL:OBX28978.1};
OS Acinetobacter gandensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1443941 {ECO:0000313|EMBL:OBX28978.1, ECO:0000313|Proteomes:UP000185753};
RN [1] {ECO:0000313|EMBL:OBX28978.1, ECO:0000313|Proteomes:UP000185753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 4275 {ECO:0000313|EMBL:OBX28978.1,
RC ECO:0000313|Proteomes:UP000185753};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBX28978.1}.
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DR EMBL; LZDS01000013; OBX28978.1; -; Genomic_DNA.
DR RefSeq; WP_067763270.1; NZ_VZOF01000026.1.
DR AlphaFoldDB; A0A1A7RBZ5; -.
DR STRING; 1443941.A9J31_14545; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000185753; 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: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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ SEQUENCE 595 AA; 64696 MW; CB7B84751333CCF7 CRC64;
MNNQSKRIFL RSQEWFDDPE HADMTALYVE RYMNYGLTRD ELQSGRPIIG IAQTGSDLTP
CNRHHKELAE RVKAGIRDAG GIPMEFPVHP IAEQSRRPTA ALDRNLAYLG LVEILHGYPL
DGVVLTTGCD KTTPACLMAA ATTDLPAIVL SGGPMLDGHY KGDLIGSGTV IWHARNLLAS
GEIDYEGFME MTTSASPSVG HCNTMGTALS MNALAEALGM SLPTCASIPA PYRERGQMAY
ATGKRICEMV LEDLRPSKIM TKKSFENAIA VASALGASSN CPPHLIAIAR HMGIELTLDD
WQRVGENIPL LVNCMPAGKY LGEGFHRAGG VPAVMYELQK AGVLHEDCAT VSGKTIGEIA
KQSKTSNADV IYPFQEPLKH GAGFIVLSGN FFDSAIMKMS VVGEAFRKTY LSNPQDENSF
EARAIVFEGP EDYHARINDP DLNIDENCIL VIRGAGTVGY PGSAEVVNMA PPTELIKKGI
DSLPCLGDGR QSGTSASPSI LNMSPEAAIG GGIALLKTND RLRIDLNKRS VNVLVSDEEL
ERRRQQWKPD YPASQTPWQE MYRKLVGQLS TGGCLEPATL YMRVINDKNL PRHSH
//