ID G2KSX3_MICAA Unreviewed; 927 AA.
AC G2KSX3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
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 Name=acnA {ECO:0000313|EMBL:AEP10118.1};
GN OrderedLocusNames=MICA_1807 {ECO:0000313|EMBL:AEP10118.1};
OS Micavibrio aeruginosavorus (strain ARL-13).
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Micavibrio.
OX NCBI_TaxID=856793 {ECO:0000313|EMBL:AEP10118.1, ECO:0000313|Proteomes:UP000009286};
RN [1] {ECO:0000313|EMBL:AEP10118.1, ECO:0000313|Proteomes:UP000009286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARL-13 {ECO:0000313|EMBL:AEP10118.1,
RC ECO:0000313|Proteomes:UP000009286};
RX PubMed=21936919; DOI=10.1186/1471-2164-12-453;
RA Wang Z., Kadouri D., Wu M.;
RT "Genomic insights into an obligate epibiotic bacterial predator: Micavibrio
RT aeruginosavorus ARL-13.";
RL BMC Genomics 12:453-453(2011).
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}.
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DR EMBL; CP002382; AEP10118.1; -; Genomic_DNA.
DR RefSeq; WP_014103341.1; NC_016026.1.
DR AlphaFoldDB; G2KSX3; -.
DR STRING; 856793.MICA_1807; -.
DR KEGG; mai:MICA_1807; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_5; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000009286; 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: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.
DR PROSITE; PS01244; ACONITASE_2; 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, ECO:0000313|EMBL:AEP10118.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009286}.
FT DOMAIN 77..588
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 718..845
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 927 AA; 100759 MW; 2222B03DDF9D3359 CRC64;
MTRTGHDSLK TRKSLTVDGK SYDYFSLPDA AKQIGDVSRL PFSMKVLLEN LLRFEDGVSV
TVDDVKACHA WLENKGKTEH EVAYRPARVL MQDFTGVPAV VDLAAMREAM KALGGNAQKI
NPLTAVDLVI DHSVMVDAFG NGAAFQTNVD REFERNGERY AFLRWGQQAF RNFRVVPPGT
GICHQVNLEY LAQTVWVEKD EERGSNVAYP DTLVGTDSHT TMVNGLAVLG WGVGGIEAEA
AMLGQPVSML IPQVIGFKIT GKMKEGTTAT DLVLTVTEML RKKGVVNKFV EFYGPGLDNM
SLADRATIGN MAPEYGATCG FFPIDRETIR YLTFTGRDPH RAKLVEEYAK AQGMWRDESS
PEPVFTDTLE LDLGAIEPSI AGPKRPQDRV VLSQAAASFK TYLADSLGVL PHDNGDARMV
SEMPESSDAA AKHDTTHAVP VEGTDYSLKH GDVVIAAITS CTNTSNPSVM LAAGLVAKKA
HERGMKVKPW VKTSLAPGSQ VVTDYLDKAG LTTHLDAMGF NLVGYGCTTC IGNSGPLPDA
IAKAVETGDL TVAGVLSGNR NFEGRINPHV KANYLASPPL VVAYALAGNM KINLATEALG
NDKDGKPVFL KDIWPTNEEI ADAVNRNLTS AMFSSRYKDV FLGPKEWQAV KGGEGETYDW
DAKSTYVANP PYFTGMSKTP PGIKDIKGAA CMALFGDSIT TDHISPAGSI KKDSPAGKYL
IEHGVDVRDF NSYGARRGHH EVMMRGTFAN IRIKNEMLGG KEGGYTKYLP TGEEMPIYDA
CMKYIKDGTP LIVVAGKEYG TGSSRDWAAK GTFLLGVKCV LAESFERIHR SNLVGMGVLP
LMFKNGQTRQ SLKLDGTETF DILGLEKGIK PRMDVTVTIT RKDGSKEEIQ ALCRIDTQDE
IGYYENGGIM HYVLRDLAAK SAKEKVA
//
