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Database: UniProt
Entry: A0A166UKM1_9GAMM
LinkDB: A0A166UKM1_9GAMM
Original site: A0A166UKM1_9GAMM 
ID   A0A166UKM1_9GAMM        Unreviewed;       936 AA.
AC   A0A166UKM1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Aconitate hydratase {ECO:0000313|EMBL:KZN30783.1};
GN   ORFNames=N475_23925 {ECO:0000313|EMBL:KZN30783.1};
OS   Pseudoalteromonas luteoviolacea DSM 6061.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1365250 {ECO:0000313|EMBL:KZN30783.1, ECO:0000313|Proteomes:UP000076643};
RN   [1] {ECO:0000313|EMBL:KZN30783.1, ECO:0000313|Proteomes:UP000076643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6061 {ECO:0000313|EMBL:KZN30783.1,
RC   ECO:0000313|Proteomes:UP000076643};
RA   Vynne N.G., Mansson M., Gram L.;
RT   "Comparative Genomic and Metabolomic Analysis of Twelve Strains of
RT   Pseudoalteromonas luteoviolacea.";
RL   Submitted (JUL-2013) 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:KZN30783.1}.
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DR   EMBL; AUYB01000146; KZN30783.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166UKM1; -.
DR   STRING; 43657.S4054249_14330; -.
DR   PATRIC; fig|1365250.3.peg.4741; -.
DR   Proteomes; UP000076643; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076643}.
FT   DOMAIN          7..163
FT                   /note="Aconitase B HEAT-like"
FT                   /evidence="ECO:0000259|Pfam:PF11791"
FT   DOMAIN          177..406
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   936 AA;  101154 MW;  D3C2A8E4C34A5A67 CRC64;
     MSLYTEYLDE IQTRKTEQGL NPKPIDSAEL LSEIIAQIKD AGHEHREDSL KFFIYNTLPG
     TTSAAGVKAQ FLKEIILGEE TVAEITAEFA FELLSHMKGG PSIAVLLDLA LGNDEAVAKQ
     AAEVLKTQVF LYDADTARLQ DAFKAGNAVA KDILESYAKA EFFTKLPDVA EKIEVVTFIA
     GEGDISTDLL SPGHQAHSRA DRELHGQCMI TPEAQQEIVA LKEKHPNAKV MLIAEKGTMG
     VGSSRMSGVN NVALWAGTQA SPYVPFINIA PVVAGTNGIA PIFLTTVDVT GGIGLDLKNW
     VKKVDENGNT VTDQNGDPVL EEAYSVATGT VLTIDTKAKK LFNGEEELAD ISSAFTPQKV
     EFMKAGGSYA VVFGKKLQTL AAETLGVEAP TVYAPSKEIS HEGQGLTAVE KIFNRNAVGV
     ASDTPLHAGS NVRVKVNIVG SQDTTGPMTS QELEAMAAST ISPLVDGAYQ SGCHTASVWD
     KKAQANIPKL MAFMNKFGLI TARDPKGIYH SMTDVIHKVL NDITVDDRAI IIGGDSHTRM
     SKGVAFGADS GTVALALATG ESAMPIPDSV KVTFKGKMAE HMDFRDVVHA TQAQMLKQFG
     GENVFQGRII EVHIGTLMAD QAFTFTDWTA EMKAKASICI SNDETLIKSI ELAKSRIQIM
     INKGMENEAK TLQGLIDLAD ERIAGVKSGE QPALAPDDNA KYYAEVVVDL DEIVEPMIAD
     PDVNNEDVSK RYTHDVIRPV SYYNDKPVDL GFVGSCMVHK GDMQIIAQML RNLEKQNGSI
     EFKAPLVVAP PTYNIVDELK AEGDWEILAK YAGFEFDDEK PKTAARTKYE NILYLERPGC
     NLCMGNQEKA EPGDTVIATS TRLFQGRVVA DTSEKKGESL LGSTPLVVLS TVLGRFPTMV
     EYKAAVEGID LTAFTPLEEE LTTKFGSEQA VPVKVV
//
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