ID A6ETA5_9BACT Unreviewed; 935 AA.
AC A6ETA5;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Aconitate hydratase 2 {ECO:0000313|EMBL:EDM43170.1};
GN ORFNames=SCB49_11864 {ECO:0000313|EMBL:EDM43170.1};
OS unidentified eubacterium SCB49.
OC Bacteria; Bacteroidota; environmental samples.
OX NCBI_TaxID=50743 {ECO:0000313|EMBL:EDM43170.1, ECO:0000313|Proteomes:UP000003659};
RN [1] {ECO:0000313|EMBL:EDM43170.1, ECO:0000313|Proteomes:UP000003659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCB49 {ECO:0000313|EMBL:EDM43170.1,
RC ECO:0000313|Proteomes:UP000003659};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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:EDM43170.1}.
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DR EMBL; ABCO01000010; EDM43170.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ETA5; -.
DR STRING; 50743.SCB49_11864; -.
DR Proteomes; UP000003659; Unassembled WGS sequence.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000003659};
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 177..407
FT /note="Aconitase B swivel"
FT /evidence="ECO:0000259|Pfam:PF06434"
FT DOMAIN 411..896
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
SQ SEQUENCE 935 AA; 102691 MW; EDC10EE575581122 CRC64;
MSIYKEYIEE IKERKLQGLD PKPIDGADLL VSIIEQIKDV ENEFREDSLN FFIYNVLPGT
TSAASVKAEF LKEIILGDFV LDEITPTFAY ELLSHMKGGP SIKVLLDLAL GDDASIAATA
AKVLKTQVFL YEADVERLEK AYQDGNAIAK ELLESYVEAE FFTKLPEVEE EIKVVTFIAG
VGDISTDLLS PGADAHSRSD RQLHGQCMFE HNKDMQNELL EIQKQHPDKR VMLIAEKGTM
GVGSSRMSGV NNVALWTGIP SSPYVPFINI APVIAGTNGI SPIFLTTVGV TGGIGIDLKN
WVKQKDEDGN TIVNEDGDPV LKQEYSVETG TVLTINTKTK KLYNGDTELK DISTALTPQK
MEFIRAGGSY AVVFGKKLQT LAAKILETEI PQVYASSKEI SIEGQGLTAV EKIFNKNAVG
NTPGKVLHAG SDVRVEVNIV GSQDTTGLMT SQELEMMAAT VISPIVDGAY QSGCHTASVW
DDKSRANIPR LMKFMNDFGL ITARDPKGGY HAMTDVIHKV LNDLTIDDWA IIIGGDSHTR
MSKGVAFGAD SGTVALALAT GEATMPIPES VKVTFKGEMK DHMDFRDVVH ATQSQMLQHF
GGENVFQGRI IEVHIGSLLA DQAFTFTDWT AEMKAKASIC ISQDETLIES LEIAKSRIQI
MIEKGMDNKE GVLQGLIDKA NKRIDEIKSG DKPPLAPDEN AKYYAEFVVD LDIINEPMVA
DPDVNNEDVS KRYTHDTIRE LSFYKGEKHV DLGFVGSCMV HKGDIKIVAK MLKNLEMTHG
DVTFNAPLVV TAPTYNIIDE LKEEGDWEIL QKYSSFEFDD NAPKGAARTE YENILYLERP
GCNLCMGNQE KAEKGDTVMA TSTRLFQGRV VKDSDRKKGE SLLASTPVVV LSAILGRTPT
IEEYKQAVSG ITLTKFSPPL KRLTANSRPG HLLSF
//
