ID G9ZWX7_9PROT Unreviewed; 593 AA.
AC G9ZWX7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Putative dihydroxy-acid dehydratase {ECO:0000313|EMBL:EHM02518.1};
GN ORFNames=HMPREF9946_01044 {ECO:0000313|EMBL:EHM02518.1};
OS Acetobacteraceae bacterium AT-5844.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHM02518.1, ECO:0000313|Proteomes:UP000003292};
RN [1] {ECO:0000313|EMBL:EHM02518.1, ECO:0000313|Proteomes:UP000003292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT-5844 {ECO:0000313|Proteomes:UP000003292};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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:EHM02518.1}.
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; AGEZ01000032; EHM02518.1; -; Genomic_DNA.
DR AlphaFoldDB; G9ZWX7; -.
DR STRING; 1054213.HMPREF9946_01044; -.
DR PATRIC; fig|1054213.3.peg.971; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_014271_3_1_5; -.
DR OrthoDB; 9807077at2; -.
DR BioCyc; ABAC1054213:G1H32-970-MONOMER; -.
DR Proteomes; UP000003292; 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:UP000003292}.
SQ SEQUENCE 593 AA; 63864 MW; 308274DB5EE5F30C CRC64;
MDQTKKQFRL RSQRWFDDPE DPGMTALYIE RFLNFGMTRG ELQSGKPIIG IAQTGSDIAP
CNRHHLALAE RVKAGIRDAG GIPLEFPIHP IQETGKRPTA ALDRNLAYLS LVEVLHGYPI
DGVVLTTGCD KTTPACLMGA ATVNIPAIVL SGGPMLDGHY KGRLSGSGTI VWEARKMLAA
GEIDYEGFME MVASSATSVG HCNTMGTALS MNSLAEALGM SLPGCAAIPA AYRERGQMAH
ATGMRIVDMV KENLRPSDIM TREAFENTIV LASAIGASSN CPPHLVAIAR HMGVELTTED
WQGIGADIPL LVDCQPAGRF LGEMFFRGGG VPAVMKELLD AGKLHGGVKT VTGQTLAENL
EKAPEPDRDV IRAYAQPLKE QAGFVVLSGN IFDSAVMKVS VIDKKFRERF LSDPEDVFEG
KVIVFEGPED YHDRIEDPDL GVDDHTVLVI RNCGPVGYPG SAEVVNMQPP GKLIKEGLDS
LPTMGDGRQS GTSASPSILN VSPEAAVGGG LALLKSGDPI RIDLKTRKVD LLISPEELEA
RRAAWTPPKL LNKTPWEEIY RSMVGQLGTG GCLEPATLYL NILETRGESR HNH
//