ID A0A225E6P4_9BACT Unreviewed; 800 AA.
AC A0A225E6P4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=FRUB_01133 {ECO:0000313|EMBL:OWK47434.1};
OS Fimbriiglobus ruber.
OC Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC Fimbriiglobus.
OX NCBI_TaxID=1908690 {ECO:0000313|EMBL:OWK47434.1, ECO:0000313|Proteomes:UP000214646};
RN [1] {ECO:0000313|Proteomes:UP000214646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP5 {ECO:0000313|Proteomes:UP000214646};
RA Ravin N.V., Rakitin A.L., Ivanova A.A., Beletsky A.V., Kulichevskaya I.S.,
RA Mardanov A.V., Dedysh S.N.;
RT "Genome analysis of Fimbriiglobus ruber SP5, the first member of the order
RT Planctomycetales with confirmed chitinolytic capability.";
RL Submitted (JUN-2017) 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:OWK47434.1}.
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DR EMBL; NIDE01000001; OWK47434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A225E6P4; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000214646; 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 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000214646}.
FT DOMAIN 75..568
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 698..776
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 800 AA; 85619 MW; C7992D5FF05E0CC1 CRC64;
MSANSFGAKS EMTVGGKSYT IYRLSAIEAA FPQAKKLPYS LKILLENLLR TENGLSVRKP
DIEALAKWEP KAEPDTEIGF TPARVLLQDF TGVPCVVDLA AMRDAMKQLG GDPAKINPLV
PCELVIDHSV QVDEAGTAQS FEHNTKLEYE RNQERYTFLR WGMEAFNNFK VVPPETGIVH
QVNLEFLARV TFVDGAGTAY PDTLVGTDSH TTMINGLGVL GWGVGGIEAE AAMLGQPVSM
LIPQVVGFKL HGKLKEGTTA TDLVLTVTQM LRKKGVVGKF VEFYGDGLAE LPLADRATIA
NMAPEYGATC GIFPVDAETI RYLRQTGRPD ELVELVEAYY KEQGLFFVAG SPEATYSDAL
ELDLAVVEPS LAGPSRPQDR VALKDVKKSF HDALPKLKVA AKPKAVLPVL PSGTPAADAV
EPADAAALTD GSVVIAAITS CTNTSNPSVM VAAGILAKKA AARGLTTKPW VKTSLAPGSK
VVTDYLTHSG LLPDLEKLRF YVVGYGCTTC IGNSGPLSDT VSKEIAAGGL VVSAVLSGNR
NFEGRVHAEV RANYLASPPL VVAYALAGKV DIDWDNEPVG TGSDGQEVYL KDIWPTHKEV
ATVIDHAIRK EAYQSIYGQV YDGDANWKAL NVPSGDLYAW DAKSTYIANP PYFEGMERKP
SPVTEIKGAR VLALLGDSIT TDHISPAGGI KKDSPAGAYL IANGVSPKDF NQYGARRGHH
DVMVRGTFAN VRLKNALVPG VEGGVTRHLP EGTTPTSIFD ASMQYQKDGV PLIVIGARST
APVRPATGRR RARGCWASGR
//
