ID A0A3D8YHZ3_9BACT Unreviewed; 923 AA.
AC A0A3D8YHZ3;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase {ECO:0000313|EMBL:REA64160.1};
DE EC=4.2.1.3 {ECO:0000313|EMBL:REA64160.1};
DE EC=4.2.1.99 {ECO:0000313|EMBL:REA64160.1};
GN ORFNames=DSL64_00985 {ECO:0000313|EMBL:REA64160.1};
OS Dyadobacter luteus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=2259619 {ECO:0000313|EMBL:REA64160.1, ECO:0000313|Proteomes:UP000256373};
RN [1] {ECO:0000313|EMBL:REA64160.1, ECO:0000313|Proteomes:UP000256373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS19 {ECO:0000313|EMBL:REA64160.1,
RC ECO:0000313|Proteomes:UP000256373};
RA Chen L.;
RT "Dyadobacter roseus sp. nov., isolated from rose rhizosphere soil.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-
CC aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99;
CC Evidence={ECO:0000256|ARBA:ARBA00000118};
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
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:REA64160.1}.
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DR EMBL; QNUL01000001; REA64160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8YHZ3; -.
DR OrthoDB; 9758061at2; -.
DR Proteomes; UP000256373; Unassembled WGS sequence.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:RHEA.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 3.40.1060.10; Aconitase, Domain 2; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR Gene3D; 1.25.40.310; Aconitate B, HEAT-like domain; 1.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR015933; Aconitase_B_HEAT-like_dom.
DR InterPro; IPR036288; Aconitase_B_HEAT-like_dom_sf.
DR InterPro; IPR015929; Aconitase_B_swivel.
DR InterPro; IPR015932; Aconitase_dom2.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF4; ACONITATE HYDRATASE B; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF06434; Aconitase_2_N; 1.
DR Pfam; PF11791; Aconitase_B_N; 1.
DR SUPFAM; SSF74778; Aconitase B, N-terminal domain; 1.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:REA64160.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000256373};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 6..162
FT /note="Aconitase B HEAT-like"
FT /evidence="ECO:0000259|Pfam:PF11791"
FT DOMAIN 176..405
FT /note="Aconitase B swivel"
FT /evidence="ECO:0000259|Pfam:PF06434"
FT DOMAIN 410..894
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
SQ SEQUENCE 923 AA; 100658 MW; 8611A42BD2F95C40 CRC64;
MNIYQDYIKE IEERKAQGLH PKPIDGAELL TEIIAQIKDT ANEYRADSLN FFIYNTLPGT
TSAAGVKARF LKEIILGESV VEEISPAYAL VLLSHMKGGP SIEVLLDLAL GDDLAIAKEA
AEVLKTQVFL YDADTDRLKE AFKNENPIAR EILESYAKAE FFTKLPEVAE EIKIVTFIAG
EGDISTDLLS PGNQAHSRSD RELHGLCMIT PQAQAEIKAL QAEHPDKSVM LIAEKGTMGV
GSSRMSGVNN VALWTGKQAS QYIPFVNIAP IVGGTNGISP IFLTTVDVTG GIGIDLKNWV
KKVDAEGNTV RNENGDPILE EVYSVATGTV LTINTKTKKL YNGEQELIDI SKALTPQKKE
FIKAGGSYAI VFGKKIQTIA AKILGIEPTL VFAPSKEISN EGQGLTAVEK IFNKNAVGIT
PGKVLHAGSD VRVEVNIVGS QDTTGLMTAQ ELESMAATII SPIVDGAYQS GCHTASVWDK
KAQANIPKLM KFMNDFGLIT ARDPKGEYHS MTDVIHKVLN DITIDEWAII IGGDSHTRMS
KGVAFGADSG TVALALATGE ASMPIPESVK VTFKGDMKDH MDFRDVVHAT QAQMLQQFGG
ENVFQGRIIE VHIGTLPADQ AFTFTDWTAE MKAKASINIS EDDTLIESLE IAKGRIQIMI
DKGMDNAKQV LQGLINKADK RITEIKSGEK PALVPDANAK YYAEVVIDLD VIVEPMIADP
DVNNKEVSKR YTHDTIRPIS YYGEDKKVDL GFVGSCMVHK GDLKIVSQML KNLEEQQGKV
EFHAPLVVAA PTYNIVEELK NEGDWDVLQK YSGFEFDDKA PKVVARTEYE NMMYLERPGC
NLCMGNQEKA AKGDTVLATS TRLFQGRVVE DSERKKGESL LASTPVVVLS AILGRIPSVE
EYKAAVVGID LTKFAPPTKQ LSR
//
