ID D0SQ49_ACIJU Unreviewed; 918 AA.
AC D0SQ49;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
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:EEY91872.1};
GN ORFNames=HMPREF0026_02609 {ECO:0000313|EMBL:EEY91872.1};
OS Acinetobacter junii SH205.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=575587 {ECO:0000313|EMBL:EEY91872.1, ECO:0000313|Proteomes:UP000018442};
RN [1] {ECO:0000313|Proteomes:UP000018442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH205 {ECO:0000313|Proteomes:UP000018442};
RX PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA Seifert H., Dijkshoorn L.;
RT "The success of Acinetobacter species; genetic, metabolic and virulence
RT attributes.";
RL PLoS ONE 7:E46984-E46984(2012).
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; GG705014; EEY91872.1; -; Genomic_DNA.
DR RefSeq; WP_005403681.1; NZ_GG705014.1.
DR AlphaFoldDB; D0SQ49; -.
DR HOGENOM; CLU_013476_2_1_6; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000018442; 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.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, 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|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361275};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 72..587
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 716..842
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 918 AA; 100198 MW; 2271FC79E38B5248 CRC64;
MARYSKINSF NALKTLTVAS KSYQIFSLSN AAQTLGNIDR LPKSLKVLLE NLLRFEDQKS
VKVEHIQALV DWQKTKSSEQ EIQYRPARVL MQDFTGVPAV VDLAAMRAAM AQAGGDPNRI
NPLSPVDLVI DHSVMVDHFA DENAFAENVE IEMQRNGERY QFLRWGQSAF NNFSVVPPGT
GICHQVNLEY LAQAVWLGDD DGEIFAFPDT LVGTDSHTTM INGLGVLGWG VGGIEAEAAM
LGQPVSMLIP EVIGFKLTGK LNEGITATDL VLTITQMLRQ KGVVGKFVEF YGDGLADLPL
ADRATIANMA PEYGATCGFF PVDEVTLGYL ALTGRQQDRI DLVEAYSKEQ GLWRNAGDEP
IFTDTLSLDM STVQASLAGP KRPQDRVLLS DVPKTFNALM ELTLKPAKEA KENLENEGGG
GTAVAAKQAN LPHDSPTCTL EGQSFQLNHG DVVISAITSC TNTSNPSVML AAGLLAKKAV
EKGLQRKPWV KSSLAPGSKV VTDYLAAAGL TPYLDQLGYN LVGYGCTTCI GNSGPLPEAV
EEAIQCQDLN VASVLSGNRN FEGRVHPLVK TNWLASPPLV VAYGLAGNIR TDLTTQPIGQ
GNNGEDIYLK DIWPSQAEID QVLQKVNTDM FHKEYAAVFD GDETWQAIQI PQSQTYAWQS
DSTYIRHPPF FETISQAPPK ITNIEQARIL AVLGDSVTTD HISPAGNIKK DSPAGRYLQE
QGVDAKDFNS YGSRRGNHEV MMRGTFANIR IKNEMLGGEE GGNTIYIPSN EKLAIYDASM
RYQQDKTPLV IIAGKEYGTG SSRDWAAKGT NLLGIKAVIA ESFERIHRSN LVGMGVLPLQ
FVDGQTRQTL HLTGREVISI HGLSDDIQPH QTLDVSVMRE DGSQDQFKVL CRIDTLNEVE
YFKAGGILHY VLRNLIAA
//
