ID A0A0N1BNM8_9SPHN Unreviewed; 601 AA.
AC A0A0N1BNM8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:KPF82959.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:KPF82959.1};
GN ORFNames=IP83_11290 {ECO:0000313|EMBL:KPF82959.1};
OS Novosphingobium sp. AAP93.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1523427 {ECO:0000313|EMBL:KPF82959.1, ECO:0000313|Proteomes:UP000037906};
RN [1] {ECO:0000313|EMBL:KPF82959.1, ECO:0000313|Proteomes:UP000037906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP93 {ECO:0000313|EMBL:KPF82959.1,
RC ECO:0000313|Proteomes:UP000037906};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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:KPF82959.1}.
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DR EMBL; LJHZ01000066; KPF82959.1; -; Genomic_DNA.
DR RefSeq; WP_054122319.1; NZ_LJHZ01000066.1.
DR AlphaFoldDB; A0A0N1BNM8; -.
DR STRING; 1523427.IP83_11290; -.
DR PATRIC; fig|1523427.4.peg.3133; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000037906; 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:KPF82959.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ SEQUENCE 601 AA; 63982 MW; 7A29FD5E9ADEC6ED CRC64;
MTEQNNGSSA PRLRSRAWFD NPSNPDMTAL YLERYLSFGL SVAELQSDRP IIGIAQTGSD
LAPCNRHHLV LAERIRDGIR DAGGIPIEFP IHPIQETGKR PTAALDRNLS YLSLVEVLYG
YPLDGTVLTV GCDKTTPACL MAAATVNIPA IALSVGPMLN GWFKGERTGS GTIIWKAREL
LAAGEIDYRG FIELIASSAP STGFCNTMGT ATTMNSLVEA LGMALPGSAA IPAPYRDRQQ
AAYETGLAIV EMVKADRKPS DIMTRTAFLN AIRVNSAIGG STNAPIHLNA IARHMGVDLT
LDDWQDHGAG IPLLVNLQPA GEYLGEDYYR AGGVPAVVGE LLRAGLLDGS ALFCNGRTLA
ENYADAQIAD TRVIKPLAEP LLPNAGLTVL SGNLFEAAVM KTSVISDAFR ARYLSNPDDP
DAFEGRAIVF EGPEDYHANI DNPDLDIDET CMLVIRGVGP IGYPGGAEVV NMRAPAALIR
AGVDALPCIG DGRQSGTSGS PSILNAAPEA AVGGGLALLR TGDRIRIDLK RRTAEMLVPE
DELQRRREAL GGGGVAIPAP QTPWQELHRQ ITGQYPGGAV IESAVQYQRI AQTHGLPRDS
H
//
