ID A0A0N1L4H0_9SPHN Unreviewed; 589 AA.
AC A0A0N1L4H0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:KPF56924.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:KPF56924.1};
GN ORFNames=IP65_01385 {ECO:0000313|EMBL:KPF56924.1};
OS Novosphingobium sp. AAP1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1523413 {ECO:0000313|EMBL:KPF56924.1, ECO:0000313|Proteomes:UP000037880};
RN [1] {ECO:0000313|EMBL:KPF56924.1, ECO:0000313|Proteomes:UP000037880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP1 {ECO:0000313|EMBL:KPF56924.1,
RC ECO:0000313|Proteomes:UP000037880};
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:KPF56924.1}.
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DR EMBL; LJHO01000001; KPF56924.1; -; Genomic_DNA.
DR RefSeq; WP_028657634.1; NZ_LJHO01000001.1.
DR AlphaFoldDB; A0A0N1L4H0; -.
DR STRING; 1523413.IP65_01385; -.
DR PATRIC; fig|1523413.3.peg.284; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000037880; 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:KPF56924.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000037880}.
SQ SEQUENCE 589 AA; 62693 MW; 24530EC7E13B521F CRC64;
MRSRAWFNNP ESADMTALYL ERYLNYGLTI EELQSDRPII GIAQTGSDLS PCNRHHLVLA
SRVRDGIREA GGIPIEFPLH PIQETGKRPT AGLDRNLAYL GLVEVLFGYP LDGVVLTIGC
DKTTPAALMA AATVNIPAIA LSVGPMLNGW HEGKRTGSGT IVWKAREMLS KGEIDFKGFI
ELVASSAPST GYCNTMGTAT TMNSLAEALG MSLPGSAAIP APHRDRQECA YYTGKQIVEM
VAADRKPSDI LTRSAFLNAI RVNSAIGGST NAPIHLNAIA RHVGVELTLE DWENHGADIP
LLVNLQPSGE YLGEDYFRAG GVPAVMGELA RAGLLDGAAL TANGKSVADN VAHVKIADED
VIRPFDRPLK PAAGLTVLGG NLFDAAVMKK SVISDQFRAR YLSNPDDPEA FEGQVFVFDG
PEDYHARIDD PALGIDERAI LVIRGAGPIG YPGGAEVVNM RPPAALIRAG IDALPCLGDG
RQSGTSGSPS ILNASPEAAV GGGLALLRDG DRIRVDLKTR SVNLLVSDAE LATRRAALAA
EPFRFPEDQT PWQAISRKIT GQFAGGAVIE DAVRFQKVAQ VYGVPRDSH
//
