ID A0A3L9MBU3_9FLAO Unreviewed; 920 AA.
AC A0A3L9MBU3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase {ECO:0000313|EMBL:RLZ10468.1};
DE EC=4.2.1.3 {ECO:0000313|EMBL:RLZ10468.1};
DE EC=4.2.1.99 {ECO:0000313|EMBL:RLZ10468.1};
GN ORFNames=EAH69_06670 {ECO:0000313|EMBL:RLZ10468.1};
OS Flavobacteriaceae bacterium YIM 102668.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=2479857 {ECO:0000313|EMBL:RLZ10468.1, ECO:0000313|Proteomes:UP000275348};
RN [1] {ECO:0000313|EMBL:RLZ10468.1, ECO:0000313|Proteomes:UP000275348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 102668 {ECO:0000313|EMBL:RLZ10468.1,
RC ECO:0000313|Proteomes:UP000275348};
RA Chen X.;
RL Submitted (OCT-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:RLZ10468.1}.
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DR EMBL; RDOJ01000007; RLZ10468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L9MBU3; -.
DR OrthoDB; 9758061at2; -.
DR Proteomes; UP000275348; 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:RLZ10468.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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 920 AA; 99969 MW; 73B87B0D903C6C00 CRC64;
MSLYKEYINE IEERKGQGLH PKPIDGAELL SEIIAQIKDL GNEYREDSVK FFIYNTLPGT
TSAAGVKAKF LKEIILGQEV VAEITPAFAF ELLSHMKGGP SIEVLLDIAL GENAELAQKA
AKVLKTQVFL YEADTARLAD AYNSGNAIAK DILESYAKAE FFTELPEVAE EIKVVTYIAA
EGDISTDLLS PGNQAHSRSD RELHGQCMMT PAQQQEIEAL KAAHPDASVM LIAEKGTMGV
GSSRMSGVNN VALWTGKQAS PYVPFVNIAP IVAGTNGISP IFLTTVDVTG GIGIDLQNWV
KKTDENGNVV RNEAGDIVLE EAYSVATGTV LTINTKTKKL YNGDVELKDI SKSFTPQKLE
FIKAGGSYAI VFGKKIQTFA AQTLGVEAPV VFAPAKEVSV EGQGLTAVEK IFNNNAVGVA
EGTVLHAGSD VRVKVNIVGS QDTTGLMTAQ ELEAMAATVI SPVVDGAYQS GCHTASVWDK
KAQANIPKLM KFMNDFGVIT ARDPKGVYHS MTDVIHKVLN DITIDEWAII IGGDSHTRMS
KGVAFGADSG TVALALATGE ASMPIPESVK VTFKGAMKEH MDFRDVVHAT QQQMLKQFDG
ENVFQGRIIE VHIGTLLADQ AFTFTDWTAE MKAKASICIS QDETLIQSLE IAKSRIQIMI
DKGMENKNNV LHGLIEKANT RIEEIRSGAK PALQPDANAK YYAEVVIDLD IIDEPMIADP
DVNNVDVSKR YTHDVIRELS YYGNDKTVDL GFVGSCMVHK DDLKIVSQML RNVEAQQGEV
KFNAPLVVAA PTYNIIDELK AEGDWEMLQK YSGFEFSDLL PKSEARTQYE NIMYLERPGC
NLCMGNQEKA EKGDTVLATS TRLFQGRVVE DRDGKKGESL LASTPVVVLS AILGRIPSIE
EYKAAVAGIN LTKFTPISTK
//
