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Database: UniProt
Entry: A0A1Y2L6Y5_9PROT
LinkDB: A0A1Y2L6Y5_9PROT
Original site: A0A1Y2L6Y5_9PROT 
ID   A0A1Y2L6Y5_9PROT        Unreviewed;       612 AA.
AC   A0A1Y2L6Y5;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=TALK_19955 {ECO:0000313|EMBL:OSQ43839.1};
OS   Thalassospira alkalitolerans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Thalassospiraceae; Thalassospira.
OX   NCBI_TaxID=1293890 {ECO:0000313|EMBL:OSQ43839.1, ECO:0000313|Proteomes:UP000193396};
RN   [1] {ECO:0000313|EMBL:OSQ43839.1, ECO:0000313|Proteomes:UP000193396}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 18968 {ECO:0000313|EMBL:OSQ43839.1,
RC   ECO:0000313|Proteomes:UP000193396};
RA   Lai Q., Shao Z.;
RT   "The draft genome sequence of Thalassospira alkalitolerans JCM 18968.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:OSQ43839.1}.
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DR   EMBL; JFKB01000022; OSQ43839.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2L6Y5; -.
DR   STRING; 1293890.TALK_19955; -.
DR   OrthoDB; 9807077at2; -.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000193396; 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}.
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   612 AA;  65312 MW;  C05F08BD5FD5E2F2 CRC64;
     MKRELEQITK RIVERSKPTR EAYLARIEAA ASSRPHRSSL SCGNLAHASA GCSSADKERI
     NGDEGANLGI VTSYNDMLSA HQPLGVYPDR IKKAVFEAGA TAQVAGGVPA MCDGVTQGRP
     GMELSLFSRD VIAMSTAVSL SHDVFDAALY LGVCDKIVPG LVMGALAYGH IPAVFVPAGP
     MPSGLPNDEK ARIRQLYAQG KVGRKELLEA ETASYHSPGT CTFYGTANSN QMLMEIMGLH
     LPGAAFVNPN TDLRDALTEE AARRALQITK LGNDYRPVGK ILDEKAFVNG IIGLLATGGS
     TNHTLHLPAM ARAAGIELRW DDFDELSRLV PLLCRVYPNG QADVNHFHAA GGMGFVISDL
     LKNGLLHHDV QSISTGGMAA YGTEPYLDAG KLAWRDAPKD SHDEGILRPT EKAFSADGGL
     RMLAGNLGRS VIKVSAVKPE NRVIEAPAAV FTSQEEMMQA FKDGKLHRDV ICVVRFQGPK
     ANGMPELHKL TPPLGVLQDL GYKVALVTDG RMSGASGKVP AAIHVTPEAM MNGPIGKVKD
     GDILRLDAES GELILNVTEA ELAKRDFATF DNKAEHQTGF GRELFGVFRE HVGLAELGAS
     AVLPGTVEVE VA
//
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