ID A0A0M4PM28_9GAMM Unreviewed; 871 AA.
AC A0A0M4PM28;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Aconitate hydratase {ECO:0000256|ARBA:ARBA00012926, ECO:0000256|RuleBase:RU361275};
DE Short=Aconitase {ECO:0000256|RuleBase:RU361275};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926, ECO:0000256|RuleBase:RU361275};
GN ORFNames=SP60_00885 {ECO:0000313|EMBL:ALE51929.1};
OS Candidatus Thioglobus autotrophicus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Thioglobus.
OX NCBI_TaxID=1705394 {ECO:0000313|EMBL:ALE51929.1, ECO:0000313|Proteomes:UP000058020};
RN [1] {ECO:0000313|EMBL:ALE51929.1, ECO:0000313|Proteomes:UP000058020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EF1 {ECO:0000313|EMBL:ALE51929.1,
RC ECO:0000313|Proteomes:UP000058020};
RX PubMed=26494660;
RA Shah V., Morris R.M.;
RT "Genome Sequence of 'Candidatus Thioglobus autotrophica' Strain EF1, a
RT Chemoautotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL Genome Announc. 3:e01156-15(2015).
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 -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR EMBL; CP010552; ALE51929.1; -; Genomic_DNA.
DR RefSeq; WP_053950850.1; NZ_CP010552.1.
DR AlphaFoldDB; A0A0M4PM28; -.
DR STRING; 1705394.SP60_00885; -.
DR KEGG; tho:SP60_00885; -.
DR PATRIC; fig|1705394.5.peg.177; -.
DR OrthoDB; 9764318at2; -.
DR Proteomes; UP000058020; 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:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
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; IPR012708; 2Me_IsoCit_deHydtase_FeS-dep.
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; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR02333; 2met_isocit_dHY; 1.
DR NCBIfam; TIGR01341; aconitase_1; 1.
DR PANTHER; PTHR11670:SF43; 2-METHYLCITRATE DEHYDRATASE (2-METHYL-TRANS-ACONITATE FORMING); 1.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 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.
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:UP000058020}.
FT DOMAIN 69..538
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 661..796
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 871 AA; 95374 MW; BD94B213500AD95E CRC64;
MNTNYRKQLE GTNLDYFDTR QAVEAIDSGS YARLPYTSRI LAEQLVRRCQ PDMLTDSLKQ
LIYSKQDLDF PWYPARVVCH DILGQTALVD LAGLRDAIAD QGGDPSKVNP VVPTQLIVDH
SLAVEAPGFD ADAFAKNRAI EDRRNKDRFE FIEWCKTSFQ NVDVIPAGNG IMHQINLEKM
SPVIQTREGV AFPDTCVGTD SHTPHVDALG VMAIGVGGLE AETVMLGLPS MMRLPNIIGV
KLTGKRQEGI TATDVVLAIT EFLRNQKVVS AYLEFFGEGA KSLTIGDRAT ISNMTPEYGA
SAGLFYIDEQ TIDYLKLTGR EPEQVALVEQ YAKETGLWVD DLVDAQYQRV LTFDLSSVGR
NMAGPSNPHR RLATANLTSS GIAKELDKAQ AEEAKGRMPD GAVIIAAITS CTNTSNPRNV
VAAGLVARKA NELGLVRKPW VKTSFAPGSK VAELYLKEAG LLSELEALGF GIVGFACTTC
NGMSGALDPV IRDEIIERDL YATAVLSGNR NFDGRIHPYA KQAFLASPPL VVAYAIAGTM
RFDIEQDSLG NDKDGNPITL KDIWPTDAEI DEIVKTSVKP EMFQQIYNPM FDLGTIQEAK
SPLYNWDDKS TYITRPPYWE GALAGERTMK SMRPLAVLGD NITTDHLSPS NAIMLESAAG
AYLHKMGLPE EDFNSYATHR GDHLTAQRAT FANPKLLNEM CRDGADGKTG EIKQGSLTRV
EPEGQEMRMW EAIETYMQRA QPLIIVAGAD YGQGSSRDWA AKGVRLAGVE TIIAEGFERI
HRTNLVGMGV LPLEFIKGET RVTYSIDGSE TFDVEGEIAP GSDLTVKMTR ANGELVNIPV
KCRLDTAAEV HVYSAGGVLQ RFAQDFLEEN S
//
