ID G4FAY1_9GAMM Unreviewed; 600 AA.
AC G4FAY1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:EHA14272.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:EHA14272.1};
GN ORFNames=HAL1_17826 {ECO:0000313|EMBL:EHA14272.1};
OS Halomonas sp. HAL1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=550984 {ECO:0000313|EMBL:EHA14272.1, ECO:0000313|Proteomes:UP000005692};
RN [1] {ECO:0000313|EMBL:EHA14272.1, ECO:0000313|Proteomes:UP000005692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain {ECO:0000313|Proteomes:UP000005692};
RX PubMed=22156396; DOI=10.1128/JB.06359-11;
RA Lin Y., Fan H., Hao X., Johnstone L., Hu Y., Wei G., Alwathnani H.A.,
RA Wang G., Rensing C.;
RT "Draft Genome Sequence of Halomonas sp. Strain HAL1, a Moderately
RT Halophilic Arsenite-Oxidizing Bacterium Isolated from Gold-Mine Soil.";
RL J. Bacteriol. 194:199-200(2012).
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:EHA14272.1}.
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DR EMBL; AGIB01000084; EHA14272.1; -; Genomic_DNA.
DR RefSeq; WP_008959422.1; NZ_CP130610.1.
DR AlphaFoldDB; G4FAY1; -.
DR PATRIC; fig|550984.5.peg.3448; -.
DR Proteomes; UP000005692; Unassembled WGS sequence.
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:EHA14272.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT REGION 488..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 600 AA; 65181 MW; F338C3DE1CBF990C CRC64;
MANFQRITPE QLRSRYWFDN PDHPGTTALC IERYLNYGIT LEELTSGKPI IGICQSGSDL
TPCNRHHIDL VKRVKDGIRA AGGVPFEFPM HPIHENVRRP TAALDRNLAY LGIVEVLHGY
PLDGVVLTTG CDKTTPAALM AAATVNIPAI VLSGGPMLNG WRGAERVGSG TIIWELRKRL
AAGDIDYAEF LSRASDSAPS IGHCNTMGTA STMNSMAEVL GMSLPGSAVI PAPYKERAMV
AYDTGTRIVD MVWEDLRPLD ILTREAFENA IVACSALGGS SNAPVHINAI ARHAGIELDN
DDWQRLGHEI PLLANVMPAG AFLCEEFHRA GGVPAILHEL HTAGKLHSDA LTVNGRSIGD
NLQGRETQDI DVICRYNDPL VNHAGFLNLK GNLFDSALMK TSVISRDFRD RFLNDPSDPE
AFEGKVVVFD GSEDYHARID DPALNIDART ILVMRGAGPV GHPGGAEVVN MQPPEALIKQ
GIESLPCLGD GRQSGTSGSP SILNASPEAA TGGGLALLES GDRLRVDLKR GEVQLLIEAS
ELEARRERLA QQGGYRYPGH QTPWQEIQRS MVEPLDRGMT LEPATKYRDV ARRHPPRDNH
//
