ID G6A1B9_9PROT Unreviewed; 601 AA.
AC G6A1B9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Dihydroxyacid dehydratase/phosphogluconate dehydratase {ECO:0000313|EMBL:EHI48504.1};
GN ORFNames=HIMB100_00020880 {ECO:0000313|EMBL:EHI48504.1};
OS SAR116 cluster alpha proteobacterium HIMB100.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster.
OX NCBI_TaxID=909943 {ECO:0000313|EMBL:EHI48504.1, ECO:0000313|Proteomes:UP000004261};
RN [1] {ECO:0000313|EMBL:EHI48504.1, ECO:0000313|Proteomes:UP000004261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain HIMB100 {ECO:0000313|Proteomes:UP000004261};
RX PubMed=22675578; DOI=10.4056/sigs.1854551;
RA Grote J., Bayindirli C., Bergauer K., Carpintero de Moraes P., Chen H.,
RA D'Ambrosio L., Edwards B., Fernandez-Gomez B., Hamisi M., Logares R.,
RA Nguyen D., Rii Y.M., Saeck E., Schutte C., Widner B., Church M.J.,
RA Steward G.F., Karl D.M., Delong E.F., Eppley J.M., Schuster S.C.,
RA Kyrpides N.C., Rappe M.S.;
RT "Draft genome sequence of strain HIMB100, a cultured representative of the
RT SAR116 clade of marine Alphaproteobacteria.";
RL Stand. Genomic Sci. 5:269-278(2011).
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:EHI48504.1}.
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DR EMBL; AFXB01000010; EHI48504.1; -; Genomic_DNA.
DR AlphaFoldDB; G6A1B9; -.
DR STRING; 909943.HIMB100_00020880; -.
DR PATRIC; fig|909943.3.peg.2152; -.
DR eggNOG; COG0129; Bacteria.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000004261; Unassembled WGS sequence.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000004261}.
SQ SEQUENCE 601 AA; 64620 MW; 6491A7E6BD2CCCA0 CRC64;
MADRKIKPEN LRSRLWFNNP DDAEMTALYT ERYLNYGLTR DELRAGKPII GIAQTGSDLS
PCNRHHLELA KRVRDGIISA GGVPMEIPVH PIQETGKRPT AMLDRNLAYL SLVESLYGYP
IDGVVLMIGC DKTTPALLMA AATVDIPAIA LSVGPMLNGW HDGERTGSGT IVWKARQLMA
AGEIDDDGFL DLVTSSTPST GYCNTMGTAT TMNSLAEALG MQLPGSAAIP APYRERGQIS
YETGARIVDM VWDDLKPSDI MTRQAFENAI AVNSAIGGST NAPIHLNAIA RHLGVPLTND
DWQAVGHQIP LLVNLQPAGE YLGEDYHRAG GVPAVVAEMM RHNLLPHPGA VTANGQSIGQ
NCAEARIKNA AVIFSVDKPM KQAAGFINLK GNLFDSAIMK TSVISQAFAD RYLSNPDDIN
AFEGTAFVFD GPEDFHHRID DESLNMDENS ILVMRGAGPI GYPGGAEVVN MRPPAYLIKK
GVAELPCIGD GRQSGTSGSP SILNASPEAA AGGGLALLRS GDQIRIDMNK CTADILISDD
ELAARREELA AQGGFASPDS QSPWQQYFRE MVTPFSEGMV LRDAPDYKSI ARTKGVPRDN
H
//
