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Database: UniProt
Entry: S6HG39_9GAMM
LinkDB: S6HG39_9GAMM
Original site: S6HG39_9GAMM 
ID   S6HG39_9GAMM            Unreviewed;       936 AA.
AC   S6HG39;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Aconitase B {ECO:0000313|EMBL:EPJ43917.1};
GN   ORFNames=OFPII_38510 {ECO:0000313|EMBL:EPJ43917.1};
OS   Osedax symbiont Rs1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae.
OX   NCBI_TaxID=1330036 {ECO:0000313|EMBL:EPJ43917.1, ECO:0000313|Proteomes:UP000014822};
RN   [1] {ECO:0000313|EMBL:EPJ43917.1, ECO:0000313|Proteomes:UP000014822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rs1 {ECO:0000313|Proteomes:UP000014822};
RA   Yi H., Goffredi S.;
RT   "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT   Osedax worms: functional variation and environmental selection.";
RL   Submitted (MAY-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:EPJ43917.1}.
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DR   EMBL; ASZJ01000182; EPJ43917.1; -; Genomic_DNA.
DR   AlphaFoldDB; S6HG39; -.
DR   PATRIC; fig|1330036.3.peg.3689; -.
DR   Proteomes; UP000014822; 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:UP000014822};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
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          410..894
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
SQ   SEQUENCE   936 AA;  101763 MW;  5023CE74B80EFCD2 CRC64;
     MNLYLDYIEE IKSRKTDLGL APLPIDSSEL LTEIITQIKD LGNEHREDSL NFFIYNTLPG
     TTSAAGVKAK FLKEIILAES VVAEITPSFA FELLSHMKGG PSVEVLLDLS LGDDAAIATS
     AAEVLKTQVF LYDADTERLA TAFKNGNSIA KDVLESYARA DFFTKLPEID EEIDVVTYIA
     AEGDISTDLL SPGNQAHSRS DRELHGKCMI SPEAQAKIEE FKTLYPGKKV MLIAEKGTMG
     VGSSRMSGVN NVALWAGEQA SPYIPFVNFA PVVAGTNGIS PIFLTTVGVT GGIGLDLKNW
     VKKLDANGKT VLNDNGDPVL VQSYSVETGT VLTINTKQKK LYKGDQELVD ISSAFTPQSV
     EFMKAGGSYA IVFGKKLQNF ASQTLSIALK PVFAPSQEIS HAGQGLTAVE KIFNKNAVGV
     TEGAVLHAGS DVRVTVNIVG SQDTTGLMTS QELESMAATT ISPIVDGAYQ SGCHTASVWD
     KKAQANIPKL MSFMHNFGLI TARDPEGVYL PMTDVIHKVL NDITIDEWAI IIGGDSHTRM
     SKGVAFGADS GTVALALATG EATMPIPESV KVTFKGKMKG HIDFRDVVHA TQSQMLKQFG
     DNIFQGRIIE VHIGTLLADQ AFTFTDWTAE MKAKGSICIS QDDKLIESLE IAKSRIQIMI
     NKGMENDARV LHGLIAKADQ RISEITSGEI PALKPDNNAK YYSELVVDLD LIDEPMIADP
     DVNNEDVSKR YTHDVIRQLS YYDGSRDVDL GFVGSCMVHK GDLQIISQMF RNIEAKNGSI
     EFKAPLIVAA PTYNIIDELK AEGDWDILQK YSGFEFDDSN PKESARTKYE NMMYLERPGC
     NLCMGNQEKA EKGDTVLATS TRLFQGRVVE DSERKKGESL LASTPVVVLS AILGRTPSMD
     EYKKAVDGIN LTDFAPPLEA MTTTPTAVPV KIMNPM
//
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