GenomeNet

Database: UniProt
Entry: I8UDJ8_9ALTE
LinkDB: I8UDJ8_9ALTE
Original site: I8UDJ8_9ALTE 
ID   I8UDJ8_9ALTE            Unreviewed;       610 AA.
AC   I8UDJ8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Phosphogluconate dehydratase {ECO:0000256|HAMAP-Rule:MF_02094};
DE            EC=4.2.1.12 {ECO:0000256|HAMAP-Rule:MF_02094};
GN   Name=edd {ECO:0000256|HAMAP-Rule:MF_02094};
GN   ORFNames=AGRI_02810 {ECO:0000313|EMBL:EIW90078.1};
OS   Alishewanella agri BL06.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alishewanella.
OX   NCBI_TaxID=1195246 {ECO:0000313|EMBL:EIW90078.1, ECO:0000313|Proteomes:UP000035062};
RN   [1] {ECO:0000313|EMBL:EIW90078.1, ECO:0000313|Proteomes:UP000035062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL06 {ECO:0000313|EMBL:EIW90078.1,
RC   ECO:0000313|Proteomes:UP000035062};
RX   PubMed=22933763; DOI=10.1128/JB.01129-12;
RA   Kim J., Jung J., Sung J.S., Chun J., Park W.;
RT   "Genome Sequence of Pectin-Degrading Alishewanella agri, Isolated from
RT   Landfill Soil.";
RL   J. Bacteriol. 194:5135-5136(2012).
CC   -!- FUNCTION: Catalyzes the dehydration of 6-phospho-D-gluconate to 2-
CC       dehydro-3-deoxy-6-phospho-D-gluconate. {ECO:0000256|HAMAP-
CC       Rule:MF_02094}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=6-phospho-D-gluconate = 2-dehydro-3-deoxy-6-phospho-D-
CC         gluconate + H2O; Xref=Rhea:RHEA:17277, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57569, ChEBI:CHEBI:58759; EC=4.2.1.12;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02094};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02094};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_02094};
CC   -!- PATHWAY: Carbohydrate metabolism; Entner-Doudoroff pathway.
CC       {ECO:0000256|HAMAP-Rule:MF_02094}.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC       {ECO:0000256|ARBA:ARBA00006486, ECO:0000256|HAMAP-Rule:MF_02094}.
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:EIW90078.1}.
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; AKKU01000006; EIW90078.1; -; Genomic_DNA.
DR   RefSeq; WP_008983502.1; NZ_AKKU01000006.1.
DR   AlphaFoldDB; I8UDJ8; -.
DR   STRING; 1195246.AGRI_02810; -.
DR   PATRIC; fig|1195246.3.peg.550; -.
DR   eggNOG; COG0129; Bacteria.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000035062; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004456; F:phosphogluconate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046177; P:D-gluconate catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009255; P:Entner-Doudoroff pathway through 6-phosphogluconate; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.30.80; IlvD/EDD C-terminal domain-like; 1.
DR   HAMAP; MF_02094; Edd; 1.
DR   InterPro; IPR004786; 6-phosphgluc_deHydtase.
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   NCBIfam; TIGR01196; edd; 1.
DR   PANTHER; PTHR43661; D-XYLONATE DEHYDRATASE; 1.
DR   PANTHER; PTHR43661:SF1; PHOSPHOGLUCONATE DEHYDRATASE; 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   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_02094};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_02094};
KW   Gluconate utilization {ECO:0000256|ARBA:ARBA00023064, ECO:0000256|HAMAP-
KW   Rule:MF_02094}; Iron {ECO:0000256|HAMAP-Rule:MF_02094};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_02094};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02094};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02094};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035062}.
FT   BINDING         154
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
FT   BINDING         221
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02094"
SQ   SEQUENCE   610 AA;  64872 MW;  5B3D1E15202AD7C3 CRC64;
     MNPVIQRVTD RIIARSSKSR AIYLDRLEEA RRKGPHRGAL SCGNLAHGFA ACNASEKSDL
     RSLTKANIAI ISSYNDMLSA HQPYQFYPEI IKKAVAEVGS VAQFAGGVAA MCDGVTQGQP
     GMELSLISRD NIAMAAAIGL SHNMFDGGLM LGICDKIVPG LLLAALSFGH LPFVFVPAGP
     MPSGIPNKEK ARVRQLFAEG KVGKEELLEA EAKSYHAAGT CTFYGTANSN QLVVEVMGLH
     LPGSSFINPY TPLRDELTRA AARQVTRLTD LGTDYLPIGK LVDAKVVVNG IVGLLATGGS
     TNHTMHLIAV ARAAGFIVNW DDFAELSQAT PLLAKIYPNG QADINHFQHA GGVPLLIRTL
     LDAGLLHEDV QTVAGFGLRR YTQQPLLENG ELRWVDAPLQ SQDPDVLTTV DKPFKATGGL
     QVLSGNIGRA VLKTSALRPG TEVVKAPAVV FHSQHELEAA FKAGELNKDC VVVVRFQGPK
     ACGMPELHKL TPPLGVLQDK GFKVALVTDG RMSGASGKVP AAIHVTPEAL DGGNIARIQT
     GDLLLVDGET GKLEVLVDAA EFAARTPATA DLSHNLYGMG REMFGAMRLQ LTGAEQGACS
     LFVTEEHLHG
//
DBGET integrated database retrieval system