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Database: UniProt
Entry: A0A0D6N0I6_9PROT
LinkDB: A0A0D6N0I6_9PROT
Original site: A0A0D6N0I6_9PROT 
ID   A0A0D6N0I6_9PROT        Unreviewed;       929 AA.
AC   A0A0D6N0I6; A0A6N3SQ85;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase {ECO:0000313|EMBL:GAN59083.1};
GN   ORFNames=Abci_001_099 {ECO:0000313|EMBL:GAN59083.1};
OS   Acetobacter cibinongensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=146475 {ECO:0000313|EMBL:GAN59083.1, ECO:0000313|Proteomes:UP000032671};
RN   [1] {ECO:0000313|EMBL:GAN59083.1, ECO:0000313|Proteomes:UP000032671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4H-1 {ECO:0000313|EMBL:GAN59083.1,
RC   ECO:0000313|Proteomes:UP000032671};
RA   Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT   "Whole genome sequence of Acetobacter cibinongensis 4H-1.";
RL   Submitted (NOV-2012) 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:GAN59083.1}.
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DR   EMBL; BAMV01000001; GAN59083.1; -; Genomic_DNA.
DR   RefSeq; WP_048837179.1; NZ_BJVU01000005.1.
DR   AlphaFoldDB; A0A0D6N0I6; -.
DR   STRING; 1231339.Abci_001_099; -.
DR   Proteomes; UP000032671; 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:0003723; F:RNA 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}.
FT   DOMAIN          7..162
FT                   /note="Aconitase B HEAT-like"
FT                   /evidence="ECO:0000259|Pfam:PF11791"
FT   DOMAIN          175..405
FT                   /note="Aconitase B swivel"
FT                   /evidence="ECO:0000259|Pfam:PF06434"
FT   DOMAIN          411..894
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
SQ   SEQUENCE   929 AA;  100530 MW;  1EFC5E4364CB2818 CRC64;
     MTAYSDYLID IKERATHGLA PKPIDDGELV RDIITLIEDT GNEQRSDALR FFIYNTLPGT
     TSAAGVKADF LKKIVQGAVV VPEITPAYAL ELLSHMKGGP SVRVLLDIAL GTDPAIAKQA
     GEVLKTQVFL YDADMFRLRD AYKAGNAVAK DVLESYAKAE FFTKLPDVED AIKVVTFIAA
     EGDISTDLLS PGNQAHSRSD RELHGQCMIS PEAQQDIVAL QKQHPDARVM MIAEKGTMGV
     GSSRMSGVNN VALWTGKQAS PYVPFVNFAP IVAGTNGISP IFATTVDVTG GIGINLKNWV
     RKTGADGKPV LDSDGNPILE QKYSVATGTV LTIDVKNKQL RDENGKELVD IASSFTPQKM
     EFMKAGSSYA IVFGKKLQTF AAKTLGIEAP RVFALNKEIT VENQGLTAVE KIFNRNAVGV
     TPGKVLHAGS DVRVQVNIVG SQDTTGLMTA QELEAMAATV ISPLVDGAYQ SGCHTASVWD
     KKAQANIPKL MKFMNDFGLI TARDPKGVYP PMTDVIHKVL NDLTVSDWDI IIGGDSHTRM
     SKGVAFGADS GTVALALATG EATMPIPQSV KVTFKGTMQP HMDFRDVVHA TQAQMLKQCG
     DNVFQGRIIE VHIGTLLADQ AFTFTDWTAE MKAKAAICIS QDEALIESLE IAKSRIQIMI
     DKGMDNAAGI LKGLIAKADK RIAEIRSGEN PALAPDDNAK YFAEVVVDLD VIDEPMIADP
     DVNNPDVSKR YTHDTIRPVS YYGDHKKVDL GFVGSCMVHK GDVKIVAQML KNLEAASGKV
     EFGAPLVVAA PTYNIIDELK AEGDWEILER YSGFEFNDQH PKSAARTEYE NILYLERPGC
     NLCMGNQEKA EKGDTVLATS TRLFQGRVVE DSSEKKGESL LASTPVVVLS AILGRIPTND
     EYKAAVEGIE LTRFAPPKAA LFDPLSVHY
//
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