ID A0A167V221_9FLAO Unreviewed; 923 AA.
AC A0A167V221;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Aconitate hydratase {ECO:0000313|EMBL:OAB26008.1};
GN ORFNames=FBFR_13610 {ECO:0000313|EMBL:OAB26008.1};
OS Flavobacterium fryxellicola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=249352 {ECO:0000313|EMBL:OAB26008.1, ECO:0000313|Proteomes:UP000077164};
RN [1] {ECO:0000313|EMBL:OAB26008.1, ECO:0000313|Proteomes:UP000077164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16209 {ECO:0000313|EMBL:OAB26008.1,
RC ECO:0000313|Proteomes:UP000077164};
RA Shin S.-K., Yi H.;
RT "Draft genome sequence of Flavobacterium fryxellicola DSM 16209.";
RL Submitted (MAR-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}.
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:OAB26008.1}.
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DR EMBL; LVJE01000038; OAB26008.1; -; Genomic_DNA.
DR RefSeq; WP_066082376.1; NZ_LVJE01000038.1.
DR AlphaFoldDB; A0A167V221; -.
DR STRING; 249352.SAMN05444395_10524; -.
DR OrthoDB; 9758061at2; -.
DR Proteomes; UP000077164; 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 RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 6..162
FT /note="Aconitase B HEAT-like"
FT /evidence="ECO:0000259|Pfam:PF11791"
FT DOMAIN 178..404
FT /note="Aconitase B swivel"
FT /evidence="ECO:0000259|Pfam:PF06434"
FT DOMAIN 409..894
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
SQ SEQUENCE 923 AA; 100221 MW; 5629F17ADFC8A002 CRC64;
MNIYNDYLKE IEERKGQGLH PKPIDGAELL GEIITQIKDL DNANREDSLS FFIYNTVPGT
TPAAGRKAAF LKEIILGIYD IKEITPVFAF ELLSHMKGGP SIKVLLDLAL DTNVAIAKEA
AEVLKTQFFL YEADTNRLEL AFKSGNKVAK EILESYAKAE FFTKLPEVVA EIKVVTYIAG
EGDISTDLLS PGNQAHSRSD RELHGKCLIS PAAQDEIQAL QAQHPDKSVM LIAEKGTMGV
GSSRMSGVNN VALWTGKKAS PYVPFINSAP IVAGTNGISP IFLTTVDVTG GIGLDLKNWV
KKLDENGNPI RNESGDVVLE EAYSVATGTV LTINTKTKKL YNGDTELIDI SKAFTPQKME
FIKAGGSYAI VFGKKLQTFA SKTLGIAIVP VFAPSKEVSI DGQGLTAVEK IFNKNAVGST
PGKVLHAGSD VRVTVNIVGS QDTTGLMTSQ ELESMAATVI SPIVDGAYQS GCHTASVWDN
KSKANIPRLM QFMNDFGLIT ARDPKGIYHA MTDVIHKVLN DITVDEWAII IGGDSHTRMS
KGVAFGADSG TVALALATGE ASMPIPESVK VTFKGDMKNY MDFRDVVHAT QSQMLKQFGG
ENVFQGRIIE VHLGTLTADQ AFTFTDWTAE MKAKASICIS EDDTLIESLE IAKRRIQIMI
DKGMDNEKQV LKGLIAIANN RIAAIQSGEK PALTPDANAK YYAEVVIDLD IVVEPMIADP
DVNNADISKR YTHDTIRPLS FYGGVKKVDL GFVGSCMVHK GDLKILSQML KNIDEQYGKV
EFKAPLVVAP PTYNIVDELK AEGDWEVLQK YSGFEFDDTA PKGVARTGYE NILYLERPGC
NLCMGNQEKA AKGDTVMATS TRLFQGRVVE DTEGKKGESL LSSTPVVVLS TILGRTPTME
EYKAAVKGIN LTQFAPSHKL LVK
//
