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Database: UniProt
Entry: A0A1G6X9X6_9RHOB
LinkDB: A0A1G6X9X6_9RHOB
Original site: A0A1G6X9X6_9RHOB 
ID   A0A1G6X9X6_9RHOB        Unreviewed;       593 AA.
AC   A0A1G6X9X6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:SDD74908.1};
GN   ORFNames=SAMN04488239_11018 {ECO:0000313|EMBL:SDD74908.1};
OS   Ruegeria marina.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=639004 {ECO:0000313|EMBL:SDD74908.1, ECO:0000313|Proteomes:UP000199628};
RN   [1] {ECO:0000313|Proteomes:UP000199628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9108 {ECO:0000313|Proteomes:UP000199628};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC       {ECO:0000256|ARBA:ARBA00006486}.
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DR   EMBL; FMZV01000010; SDD74908.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6X9X6; -.
DR   STRING; 639004.SAMN04488239_11018; -.
DR   OrthoDB; 9807077at2; -.
DR   Proteomes; UP000199628; 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:UP000199628}.
SQ   SEQUENCE   593 AA;  64035 MW;  B2BD8962F4C627E8 CRC64;
     MTKRRLRSQF WFDNPDNREM TALYLERYLN YGLTWEELQS GKPIIAIAQT GSDLSPCNRH
     HVELSKRVRD GIISAGGTVI EVPVHPIQET GKRPTAMLDR NLAYLSLVET LFGYPLDGVV
     LNIGCDKTTP ALLMAAATVN IPAIAFSVGP MLNGWFRGER TGSGTIVWKA RELLAAGEID
     DAGFMELVAS SAPSVGYCNT MGTASTMNSL AEALGMQLPG SAAIPAPYRE RGQMAYETGR
     RIVEMVHEDL KPSAIMTRAA FENAIVVNSA IGGSTNAPIH LNGIARHLGV PLDNDDWQRL
     GHKVPLLVNL QPAGEYLAED YHRAGGVPAV VGELLAEGLL PHPGASTVNG RSMGENCDGR
     RSENPAVIKP VAAPMKRDAG FINLKGNLFD SAIMKTSVIS AEFQQRYLDN PEDPNAFEGR
     AIVFDGPEDF HARIDDESLA IDARCILIMR GSGPIGYPGG AEVVNMRPPS YLLKQGIHAL
     PCIGDGRQSG TSGSPSILNA SPEAAEGGGL ALVRTGDRLR IDLNTCTANM LVSDEELAER
     RAALPDHPFT PPSQSPWQEI FRERVRPFSE GMTLRGADAY RDIGNSAVPR DNH
//
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