ID A0A1U7GHJ7_9BACT Unreviewed; 905 AA.
AC A0A1U7GHJ7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Aconitate hydratase {ECO:0000256|RuleBase:RU361275};
DE Short=Aconitase {ECO:0000256|RuleBase:RU361275};
DE EC=4.2.1.3 {ECO:0000256|RuleBase:RU361275};
GN ORFNames=BGO49_26660 {ECO:0000313|EMBL:OJW17785.1};
OS Planctomycetales bacterium 71-10.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales.
OX NCBI_TaxID=1895807 {ECO:0000313|EMBL:OJW17785.1, ECO:0000313|Proteomes:UP000185848};
RN [1] {ECO:0000313|EMBL:OJW17785.1, ECO:0000313|Proteomes:UP000185848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=71-10 {ECO:0000313|EMBL:OJW17785.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000256|RuleBase:RU361275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00023501,
CC ECO:0000256|RuleBase:RU361275};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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:OJW17785.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MKTT01000090; OJW17785.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U7GHJ7; -.
DR STRING; 1895807.BGO49_26660; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000185848; 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:UniProtKB-UniPathway.
DR CDD; cd01586; AcnA_IRP; 1.
DR CDD; cd01580; AcnA_IRP_Swivel; 1.
DR Gene3D; 6.10.190.10; -; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR InterPro; IPR044137; AcnA_IRP_Swivel.
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; IPR006249; Aconitase/IRP2.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01341; aconitase_1; 1.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR PANTHER; PTHR11670:SF54; CYTOPLASMIC ACONITATE HYDRATASE; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|RuleBase:RU361275};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361275};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361275};
KW Lyase {ECO:0000256|RuleBase:RU361275};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 72..565
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 695..822
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 905 AA; 97696 MW; 3AE8CDCA412DE06C CRC64;
MPKSYGALTP LSVDGRTYQY YRLGALAGHG LDASRLPFSL KVLLENLLRF EDGSTVTADD
VRALAQWDPK AEPDREIAFR PSRVLLQDFT GVPAVVDLAA MRDAVKALGG DPRKINPLQP
VELVIDHSVQ VDEAGTARAL VVNAELEFER NRERYAFLRW GQNAFDNFKV VPPDTGIVHQ
VNLEYLARVV FVDDEAAEGN LAYPDTLVGT DSHTTMINGL GVLGWGVGGI EAEAAMLGQP
VSMLVPQVIG FKLSGKLPEG ATATDLVLTV TQMLRKKGVV GKFVEFYGPG LASLPLADRA
TIANMAPEYG ATCGIFPVDA ETLRYLRLSN RSEETIRLVE EYYKAQGMFH DEDTPEAEFT
DTLSLDLATV EPSIAGPRRP QDRVVLSHSK PAFEAALKEL LAARPAKVKP ADQAEADSNG
VGSELKHGSV VIAAITSCTN TSNPSVMLAA GLVAKKAVER GLDTRPWVKA SLAPGSKVVT
EYLKAAGLDE YLDRIKFNTV GYGCTTCIGN SGPLPAEISE TIQKKDLVAV AVLSGNRNFE
GRINADVRAN YLASPPLVVA YALAGTMDID LASEPLGHDK QGNPVFLKDV WPTQQEVHDA
VMNSVKAEQF RKEYGAVYEG DPAWRELPTP EGDSFAWEDS STYVKNPPYF EGMQIQPTPP
KPIQGARVLA VLGDSITTDH ISPAGNIKAD SPAGRYLIGH GVKPADFNSY GSRRGNHEVM
VRGTFANIRL RNKLAPGTEG GWTRHLPDGE VMSIFDASEK YQAAGTPLII LAGKEYGSGS
SRDWAAKGPK LLGISAVVAE SYERIHRSNL VGMGIVPLQF EHGSNAESLG LTGEEVYRIE
NPDGTLAERV ATAKSVVVAA EKADGTVVRF PARVRIDTPQ EVHYYENGGI LPYVLRQLLA
GKSEA
//
