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Database: UniProt
Entry: A0A1D9PBG4_9FLAO
LinkDB: A0A1D9PBG4_9FLAO
Original site: A0A1D9PBG4_9FLAO 
ID   A0A1D9PBG4_9FLAO        Unreviewed;       923 AA.
AC   A0A1D9PBG4;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Aconitate hydratase {ECO:0000313|EMBL:AOZ99916.1};
GN   ORFNames=BIW12_11035 {ECO:0000313|EMBL:AOZ99916.1};
OS   Flavobacterium commune.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1306519 {ECO:0000313|EMBL:AOZ99916.1, ECO:0000313|Proteomes:UP000178198};
RN   [1] {ECO:0000313|EMBL:AOZ99916.1, ECO:0000313|Proteomes:UP000178198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PK15 {ECO:0000313|EMBL:AOZ99916.1,
RC   ECO:0000313|Proteomes:UP000178198};
RA   Ekwe A., Kim S.B.;
RT   "Complete Genome Sequence of Flavobacterium sp. PK15.";
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; CP017774; AOZ99916.1; -; Genomic_DNA.
DR   RefSeq; WP_071185157.1; NZ_CP017774.1.
DR   AlphaFoldDB; A0A1D9PBG4; -.
DR   STRING; 1306519.BIW12_11035; -.
DR   KEGG; fcm:BIW12_11035; -.
DR   OrthoDB; 9758061at2; -.
DR   Proteomes; UP000178198; Chromosome.
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:UP000178198};
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..405
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   923 AA;  100222 MW;  638D972C3E237F3D CRC64;
     MNIYSDYIKE IEERKIQGLH PKPIDDAQLL SEIIAQIKDL DNANREDSLQ FFIYNTLPGT
     TSAAGEKAKF LKEIILGESV VKEITPAFAF ELLSHMKGGA SIKVLLDLAL GNDAAIAKEA
     ASVLKTQVYL YDADTSRLKE AFENGNAIAK EIIESYAKAE FFTKLPEVAE EIKVVTFIAG
     EGDISTDLLS PGNQAHSRSD RELHGKCMIT PQAQEEIKAL QAQHPDKSVM LIAEKGTMGV
     GSSRMSGVNN VALWTGKQAS PYIPFVNFAP IVGGTNGISP IFLTTVDVTG GIGLDLKNWV
     KKVDAEGNVV RNESGEPILE QAYSVATGTV LTINTKTKKL YNGDQELIDI SRSFTPQKME
     FIKAGGSYAI VFGKKLQTFA AKTLGIEAPA VFAPSKEISH EGQGLTAVEK IFNRNAVGTT
     PGKVLHAGSD VRVEVNIVGS QDTTGLMTAQ ELESMAATVI SPIVDGAYQS GCHTASVWDK
     KAQANIPKLM KFMNDFGLIT ARDPKGVYHS MTDVIHKVLN DITIDEWAII IGGDSHTRMS
     KGVAFGADSG TVALALATGE ASMPIPESVK VTFKGEMKSY MDFRDVVHAT QAQMLKQFGG
     ENVFQGRIIE VHIGTLTADQ AFTFTDWTAE MKAKASICIS EDETLIESLE IAKGRIQIMI
     DKGMDNAKQV LKGLIAKADK RIAEIRSGEK PALTPDANAK YYAEVVVDLD VIAEPMIADP
     DVNNADVSKR YTHDTIRPLS FYGGEKKVDL GFIGSCMVHK GDMKILAQML KNIEAQQGKV
     EFQAPLVVAP PTYNIVDELK AEGDWEVLQK YSGFEFDDNA PKAAARTEYE NMLYLERPGC
     NLCMGNQEKA AKGDTVMATS TRLFQGRVVE DTDTKKGESL LSSTPVVVLS TILGRTPTID
     EYTAAVDGIN LTKFAPSHKQ LVK
//
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