ID I4BXD1_ACEMN Unreviewed; 571 AA.
AC I4BXD1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Dihydroxyacid dehydratase/phosphogluconate dehydratase {ECO:0000313|EMBL:AFM21938.1};
GN OrderedLocusNames=Anamo_1329 {ECO:0000313|EMBL:AFM21938.1};
OS Acetomicrobium mobile (strain ATCC BAA-54 / DSM 13181 / JCM 12221 / NGA)
OS (Anaerobaculum mobile).
OC Bacteria; Synergistota; Synergistia; Synergistales; Acetomicrobiaceae;
OC Acetomicrobium.
OX NCBI_TaxID=891968 {ECO:0000313|EMBL:AFM21938.1, ECO:0000313|Proteomes:UP000006061};
RN [1] {ECO:0000313|Proteomes:UP000006061}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-54 / DSM 13181 / NGA
RC {ECO:0000313|Proteomes:UP000006061};
RX PubMed=23961311; DOI=10.4056/sigs.3547050;
RA Mavromatis K., Stackebrandt E., Held B., Lapidus A., Nolan M., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA Liolios K., Pagani I., Ivanova N., Mikhailova N., Huntemann M., Pati A.,
RA Chen A., Palaniappan K., Land M., Rohde M., Spring S., Goker M., Woyke T.,
RA Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of the moderate thermophile Anaerobaculum mobile
RT type strain (NGA(T)).";
RL Stand. Genomic Sci. 8:47-57(2013).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; CP003198; AFM21938.1; -; Genomic_DNA.
DR AlphaFoldDB; I4BXD1; -.
DR STRING; 891968.Anamo_1329; -.
DR KEGG; amo:Anamo_1329; -.
DR PATRIC; fig|891968.3.peg.1325; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_4_2_0; -.
DR Proteomes; UP000006061; Chromosome.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
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; 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 Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000006061}.
SQ SEQUENCE 571 AA; 62065 MW; F4D546F4EAAD2A10 CRC64;
MTQRSLFARK FWAQFDALQL GSKMDEEDII KPQILIEDVF GDSHPGSVHL NSLSEQATYG
VYQSGGTPSR YHVTDACDGC AQGHDGMNII LASREAMADM VEVHVRVYLF DGMVLLSSCD
KSIPAHLMAA ARLNIPTILV PGGSMRPGPN MTTSLVAGDI SLRQKRGEVS EQEIRDYKLT
GCPSCGACAF LGTASTMQCM AEALGLALPG SALMPATMRD IFQNARNAGR KIMELVAKGI
KTSDILTKEA FKNAIIVHGA IGGSTNATIH LPAIAQEMGI EITLEEFDEI NHKVPHIGNI
TPSGTNVTEA FWFAGGIPMV QLMLKDYLNL NVLTVTGKTL GENLKDLKDD NFFNRYIGYL
YNYGLKRDDV ITPIEKAKEK GSIAFLKGNL APEGSVFKYS ACVKNMRSHR GPARVFNCEE
DAYNAVVNNE INPGDIMIIR YEGPRGSGMP EMLATTEAIV NDKRLNGSVA LVTDGRFSGG
TSGASIGHVS PEAAVGGPIA FVKDGDIIQY DLENRSIDVI GIKGKLCSRE EVKVIFERRK
QEEGVIPRPK RVGLFKRYTE NATSAIKGAR Y
//
