ID A0A369T914_9PROT Unreviewed; 600 AA.
AC A0A369T914;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:RDD60657.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:RDD60657.1};
GN ORFNames=DRB17_17045 {ECO:0000313|EMBL:RDD60657.1};
OS Ferruginivarius sediminum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Ferruginivarius.
OX NCBI_TaxID=2661937 {ECO:0000313|EMBL:RDD60657.1, ECO:0000313|Proteomes:UP000253941};
RN [1] {ECO:0000313|EMBL:RDD60657.1, ECO:0000313|Proteomes:UP000253941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WD2A32 {ECO:0000313|EMBL:RDD60657.1,
RC ECO:0000313|Proteomes:UP000253941};
RA Wang S.;
RT "Venubactetium sediminum gen. nov., sp. nov., isolated from a marine solar
RT saltern.";
RL Submitted (JUL-2018) 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:RDD60657.1}.
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DR EMBL; QPMH01000022; RDD60657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369T914; -.
DR Proteomes; UP000253941; 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:RDD60657.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000253941}.
SQ SEQUENCE 600 AA; 64253 MW; 29331EA670A3BA72 CRC64;
MNQRDDGNGG SDNKGLRSRE WWDNRETPDM TALYLERYLN YGLTREELQS GRPIIGIAQT
GSDLTPCNRH HRRLAERVKE GVRDAGGVAL EFPVHPIQET GKRPTAALDR NLAYLGLVEV
LYGYPLDGVV LTTGCDKTTP ACLMAAATVD LPAVVLSGGP MLNGTYKGKL AGSGAVIWKA
RELYSAGLID YEEFMDMAAA SAPSEGHCNT MGTALSMNVL AEALGMSLPG SASIPAPYRE
RAQMAYRTGQ ASVAAVRNGI RPSRIITREA CENAIVATSA IGGSSNCPVH LNAIARHAGV
DLSIDDWESG HDVPLLVDCQ PAGRFLGEDF HRAGGAPAVL KEALNAGRLH GAALTVNGRT
LAENLGDIPD GDRRVIRAWN EPMQERAGFL VLRGNLFESS VLKTSAIDGA FRARYLSNAA
DPDAFEGRAI VFEGPEDYHA RINDPALAID EDCILVIRNC GPVGYPGSAE VVNMLPPDYL
VRRGVTSLPC LGDGRQSGTS GSPSLLNASP EAAAGGGLAL LRTGDRLRID LGRRRADVLL
SETELEDRRT AAKPEVPADQ TPWQAIYRRS VGQLGSGACL EDAVDFMRIA QRFGVPRHSH
//