GenomeNet

Database: UniProt
Entry: A0A061NQZ7_9BACL
LinkDB: A0A061NQZ7_9BACL
Original site: A0A061NQZ7_9BACL 
ID   A0A061NQZ7_9BACL        Unreviewed;       733 AA.
AC   A0A061NQZ7;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:GAK07068.1};
GN   ORFNames=JCM19038_787 {ECO:0000313|EMBL:GAK07068.1};
OS   Geomicrobium sp. JCM 19038.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Geomicrobium.
OX   NCBI_TaxID=1460635 {ECO:0000313|EMBL:GAK07068.1, ECO:0000313|Proteomes:UP000027014};
RN   [1] {ECO:0000313|EMBL:GAK07068.1, ECO:0000313|Proteomes:UP000027014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19038 {ECO:0000313|EMBL:GAK07068.1,
RC   ECO:0000313|Proteomes:UP000027014};
RA   Kudo T., Nakahara T., Zhang X., Taniyama S., Arakawa O., Murase S.,
RA   Nakata H., Oshima K., Suda W., Kitamura K., Iida T., Oshida Y., Inoue T.,
RA   Hongoh Y., Hattori M., Ohkuma M.;
RT   "Draft Genome Sequences of Geomicrobium sp. Strains JCM 19037, JCM 19038,
RT   JCM 19039, and JCM 19055, Isolated from Aquatic Samples.";
RL   Genome Announc. 2:e00622-14(2014).
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:GAK07068.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BAXA01000002; GAK07068.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061NQZ7; -.
DR   eggNOG; COG0129; Bacteria.
DR   Proteomes; UP000027014; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR   GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW.
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; IPR037237; IlvD/EDD_N.
DR   PANTHER; PTHR43661; D-XYLONATE DEHYDRATASE; 1.
DR   PANTHER; PTHR43661:SF3; D-XYLONATE DEHYDRATASE YAGF-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.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
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:ARBA00022714};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027014}.
SQ   SEQUENCE   733 AA;  82079 MW;  43BE3E9183036311 CRC64;
     MVKYPLITDS YNPYRDNVQG KANEPITVAG LLDRSKQVLG KSYEGSVPDW TLDEIYDRLE
     NNAPRIAIIG GSSDHPAHIM DFQTSSRAAI RIWENGGVPF YFSTPVMCDG TAQSNQGMSY
     SLQSRNAVAQ MIVNQLESHN YHGAFVIQGC DKQPLGVVSG LAHLDRLRQE RGETPFIATF
     APAHVLQGGT IPDDLWGELE EVAERAVAQG YSDIADDLND AMAYILQCSS NTSFQGVFER
     AVAHEVMSFE EHKYFEKRLA VNTCDGAGGV CAFNGTGNSS RHIVAGFGLV HPELELLTEA
     PSQDVINAAL DSFEVMLNKK EFGVSNLVAA NIRNGIRIHS SSGGSTNLMM HIVAAMLYGG
     YQFSLQDLNK LHNECKIPDL FNYSLTEDRD IYQLAMQCCD SSSRGMESLF YELLQNDVPM
     DVHALTVEGR TWMERLEKKQ GLSAENVKKN RIILSKPRRA FSGVDVLKVT SLIPLLKSVV
     CRPQLDMFDN KVAQVLYFEN EEDANKELLD DRLLENLKQR EVFQKSHLLA QLKKNDSASY
     QECLEMNTEQ LFDYMIENES LKIAIIIAGQ GPEAYGMPEM FTPMQHINTN RKMKKLATVI
     SDGRYSGVTF GAAIGHMTPE AKNNGGILYL QSGDLLHIGL RNKKIDFLEV REDHEVEVSN
     RFNQITNQRN EVANLRKERM NRRMKRVAAS NRMPYHTDAS EGVVPHLIKD EADKDYVPIL
     KSVSIANVEK ERI
//
DBGET integrated database retrieval system