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Database: UniProt
Entry: A0A2T0RYJ1_9RHOB
LinkDB: A0A2T0RYJ1_9RHOB
Original site: A0A2T0RYJ1_9RHOB 
ID   A0A2T0RYJ1_9RHOB        Unreviewed;       930 AA.
AC   A0A2T0RYJ1;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Aconitase {ECO:0000313|EMBL:PRY26202.1};
GN   ORFNames=CLV78_101297 {ECO:0000313|EMBL:PRY26202.1};
OS   Aliiruegeria haliotis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Aliiruegeria.
OX   NCBI_TaxID=1280846 {ECO:0000313|EMBL:PRY26202.1, ECO:0000313|Proteomes:UP000239480};
RN   [1] {ECO:0000313|EMBL:PRY26202.1, ECO:0000313|Proteomes:UP000239480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29328 {ECO:0000313|EMBL:PRY26202.1,
RC   ECO:0000313|Proteomes:UP000239480};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-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:PRY26202.1}.
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DR   EMBL; PVTD01000001; PRY26202.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0RYJ1; -.
DR   OrthoDB; 9758061at2; -.
DR   Proteomes; UP000239480; 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:UP000239480};
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..407
FT                   /note="Aconitase B swivel"
FT                   /evidence="ECO:0000259|Pfam:PF06434"
FT   DOMAIN          411..895
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
SQ   SEQUENCE   930 AA;  100686 MW;  B66321A4AB406615 CRC64;
     MSLYTDYLDE IGTRKAQGLS PKPIDDGALV EELVAQIKDA DSVYRADSLN FFIYNTLPGT
     TSAAGVKARF LKEIILGEAV VEEITPDFAF ELLSHMKGGP SVEVLLDLAL GEDAAIAAQA
     ADVLKTQVFL YEADTDRLEA AYTAGNAVAK DILESYAKAE FFTKLPDIDE EIKVVTYIAA
     EGDISTDLLS PGNQAHSRSD RELHGKCMIS EKAQQEIEAL KLQHPDKRVM LIAEKGTMGV
     GSSRMSGVNN VALWTGKQAS PYVPFVNIAP VVAGTNGISP IFLTTVGVTG GIGLDLKNWV
     KKVDADGKPI LNNDGNPILE QKYSVETGTV LTINTRSKKL YSEDGSEELT DVSSAFTPQK
     VEFMKAGGSY AIVFGKKLQN FAAETLGVEP TPVFAPSREI SHEGQGLTAV EKIFNKNAVG
     VSDGKVLHAG SDVRVKVNIV GSQDTTGLMT SQELEAMAAT VISPTVDGAY QSGCHTASVW
     DKKAQANIPR LMKFMNNFGL ITARDPQGVY HSMTDVIHKV LNDITVDDWD IIIGGDSHTR
     MSKGVAFGAD SGTVALALAT GEATMPIPES VKVTFKGAMK DHMDFRDVVH ATQAQMLKQF
     GDNVFQGRVI EVHIGTLLAD QAFTFTDWTA EMKAKASICI SQDETLIGSL ELAKSRIKVM
     IDKGMDNEAQ TLQGLIDKAD KRIAEIRSGE KPALTPDDNA KYFAEVVVDL DEIDEPMIAD
     PDVNNADVSK RYTHDTIRPV SYYGGDKKVD LGFVGSCMVH KGDMKIVAQM LKNLEKAQGK
     VEFNAPLVVA APTYNIIDEL KAEGDWEILQ KYSGFEFDDL MPKSAARTEY ENILYLERPG
     CNLCMGNQEK AAKGDTVLAT STRLFQGRVV EDSEEKKGES LLASTPVVVL SAILGRTPSV
     EEYKSAVEGI DLTKFAPPLE KPAGSRSAHF
//
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