ID R6T684_9FIRM Unreviewed; 573 AA.
AC R6T684;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:CDC68918.1};
GN ORFNames=BN503_01554 {ECO:0000313|EMBL:CDC68918.1};
OS Oscillibacter sp. CAG:155.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillibacter; environmental samples.
OX NCBI_TaxID=1262910 {ECO:0000313|EMBL:CDC68918.1, ECO:0000313|Proteomes:UP000017942};
RN [1] {ECO:0000313|EMBL:CDC68918.1, ECO:0000313|Proteomes:UP000017942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:155 {ECO:0000313|Proteomes:UP000017942};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDC68918.1}.
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DR EMBL; CBFT010000106; CDC68918.1; -; Genomic_DNA.
DR AlphaFoldDB; R6T684; -.
DR Proteomes; UP000017942; 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; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
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.
DR PROSITE; PS00886; ILVD_EDD_1; 1.
DR PROSITE; PS00887; ILVD_EDD_2; 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:UP000017942}.
SQ SEQUENCE 573 AA; 62123 MW; E31437FFFD8DB4EA CRC64;
MMQKSHDDRM LWAQFDALEM GTGWDDTDIE KPQIMVESVY GDSHPGSWHL NQLVEQAVYG
VYEKGGKPAK YYATDICDGC AQGHDGMNVV LASREALANM VEVHASAVPW DGMILMSSCD
KSIPAHLKAA ARMDIPTIFM PGGSMRPGPN MTTSLVAGDI SLRQKRKDAI TPQEVRDYKL
TGCPSVGACT FLGTASTMQC IAEALGMTLP GAALAPATMR DIIQYARYAG RKIMELVEKN
ITASKIMTPA AFKNAIIVHS AIGGSTNATI HLPSIARELG YDLPIELFDE INHQVPHLGN
INPSGTQLTE SFWFAGGIPM VQWMLRDMLD LDVMTVTGKT LGENLEDLHK DNWFDRNLGY
LANYGLTRDQ VIFPVEKAPE KGSVAILKGN IAPEGSVLKY SACAMNQREV VNAKARVFNC
EEDAHDAVVE NKINPGEVII IRYEGPRGCG MPEMLMTTEA IVCDERINGS VALITDGRFS
GATRGAAIGH VSPEAAAGGP IAFLEEGDLI SYSVKDRTIN MTGIHGVPCT VEEATAELAK
RAEKGILPRE PRKGFYKLYT DHALSAMKGA GLE
//