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Database: UniProt
Entry: A0A0W0VTI4_9GAMM
LinkDB: A0A0W0VTI4_9GAMM
Original site: A0A0W0VTI4_9GAMM 
ID   A0A0W0VTI4_9GAMM        Unreviewed;       616 AA.
AC   A0A0W0VTI4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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   ECO:0000313|EMBL:KTD23463.1};
GN   ORFNames=Llan_0834 {ECO:0000313|EMBL:KTD23463.1};
OS   Legionella lansingensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=45067 {ECO:0000313|EMBL:KTD23463.1, ECO:0000313|Proteomes:UP000054869};
RN   [1] {ECO:0000313|EMBL:KTD23463.1, ECO:0000313|Proteomes:UP000054869}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49751 {ECO:0000313|EMBL:KTD23463.1,
RC   ECO:0000313|Proteomes:UP000054869};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) 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:KTD23463.1}.
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DR   EMBL; LNYI01000014; KTD23463.1; -; Genomic_DNA.
DR   RefSeq; WP_028373378.1; NZ_LT906451.1.
DR   AlphaFoldDB; A0A0W0VTI4; -.
DR   STRING; 45067.Llan_0834; -.
DR   PATRIC; fig|45067.4.peg.865; -.
DR   eggNOG; COG0129; Bacteria.
DR   OrthoDB; 9807077at2; -.
DR   UniPathway; UPA00226; -.
DR   Proteomes; UP000054869; 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:UP000054869}.
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   616 AA;  66204 MW;  511B1DB5DA50855A CRC64;
     MHPIIKQVTE RITVRSKKTR GHYLKHMEEA RLKGPHRSVL QCGNLAHGFA ACHAREKADL
     RAMSKPNIAI ISAYNDMLSA HQPYENYPLI LKEAIREAGG VAQFAGGVPA MCDGITQGQP
     GMELSLMSRD IIAMSAALAL AHNMFDGGLM LGICDKIVPG LLIAALRFGH LPFIFVPAGP
     MPSGIPNKEK ARVRQLYAQG NVGREALLEV EAASYHAPGT CTFYGTANSN QLIVEVMGLH
     LPGASFVNPQ TKLREALTKA AGRKISSLTH LDNNYLPISK IIDSKAIVNG MIALLATGGS
     TNHTMHLVAV ARAAGIIIDW DDFAELSKAV PLIARIYPNG QADINQFQNA GGMAYLIRTL
     LDNHLLHNDV HTVVGSGLRQ YTQQPLVKDN ELEWVDGPIE STDPDVLTAV STPFKEQGGL
     QVLSGNLGRA IIKTSSLPPG AEVVQAPAVV FSSQHELDAA FKAGELDKDC IVVVRFQGPK
     ACGMPELHQL TPLLGVLQDR GFKVALVTDG RMSGASGKIP AAIHVTPEAV DGGMIARIKT
     GDLILVDSQS GLLEVLVPEN ELAQRLPAKQ MFPECSYGMG RELFHKFRLQ LTGAEQGASG
     LFFAEEYVDD KSALSV
//
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