ID A0A0N1LD50_9PROT Unreviewed; 895 AA.
AC A0A0N1LD50;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:KPF70384.1};
GN ORFNames=IP84_01175 {ECO:0000313|EMBL:KPF70384.1};
OS beta proteobacterium AAP99.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1523428 {ECO:0000313|EMBL:KPF70384.1, ECO:0000313|Proteomes:UP000037960};
RN [1] {ECO:0000313|EMBL:KPF70384.1, ECO:0000313|Proteomes:UP000037960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP99 {ECO:0000313|EMBL:KPF70384.1,
RC ECO:0000313|Proteomes:UP000037960};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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:KPF70384.1}.
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DR EMBL; LJIA01000001; KPF70384.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1LD50; -.
DR STRING; 1523428.IP84_01175; -.
DR PATRIC; fig|1523428.3.peg.240; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000037960; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000037960}.
FT DOMAIN 73..562
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 692..822
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 895 AA; 96465 MW; 13396543CE072D8D CRC64;
MSHNLFNTRQ SFTAGGKTGT YYSLPELAKS FPNVSKLPVS IRIVLEAVLR NCDGKKVAEE
HIKQLANWQP TAERVDEIPF VVARVVLQDF TGVPLLADLA AMRNVADKMG KNPKTIEPLV
PVDLVVDHSV MIDHFGTPDA LRKNMELEFQ RNTERYQFMK WGMQAFDTFG VVPPGIGIVH
QVNLEYLFKG LQSKGDTYYP DTLVGTDSHT TMINGVGVVG WGVGGIEAEA GMLGQPVYFL
TPDVVGVELK GKLNEGVTAT DLVLTVTQML RKHKVVGKFV EFFGEGAASL SVVDRATIAN
MAPEYGATMG FFPVDDKTVD YMKKTGRTDE QCAQFEAYFK AQGLFGMPKA GDCMYSSSLT
LDLATIVPSL AGPKRPQDRI ELPSMKSSFN SLFSAPVAEN GFGQPADKLN ARFATGNGDT
TIGNGDVLIA AITSCTNTSN PGVMLAAGVL AKKAVEKGLK VAPHIKTSLG PGSRVVEDYL
AKSGLQPYLD KLGFNVAAFG CTTCIGNAGD LAPEINETIT KNDLVCAAVL SGNRNFEARI
HPNLKANFLA SPPLVVAFAI AGKANLDLTT EPLGTGSDGQ PVFLKDVWPS SDEINAVMPF
AQDPQVFKRL YADFTKDHDL WNNVPAPSGQ VYTWPESTYI ARPPFFDEFA MQPSAVAAIS
GAKPLLILGD SVTTDHISPA GSFKETTPAG KWLGSKGVQK VDFNSYGSRR GNHDIMIRGT
FANVRVKNLM LPPKADGTRI EGGFTLLDGQ QTTVYEAAME YIKRGTPTIV IGGEEYGTGS
SRDWAAKGTQ LLGVKVVVAR SFERIHRSNL VGMGVLPLQF KAGESAESLG LTATDTFDVI
GDVSKPQSDM TLVVTRSDGS KLNVSVKSRI DTPIEVDYYK HGGILPFVLR QLLAA
//
