ID A0A0A0ED21_9RHOB Unreviewed; 924 AA.
AC A0A0A0ED21;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=ATO9_15420 {ECO:0000313|EMBL:KGM47983.1};
OS Pseudooceanicola atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=1461694 {ECO:0000313|EMBL:KGM47983.1, ECO:0000313|Proteomes:UP000030004};
RN [1] {ECO:0000313|EMBL:KGM47983.1, ECO:0000313|Proteomes:UP000030004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-s11g {ECO:0000313|EMBL:KGM47983.1,
RC ECO:0000313|Proteomes:UP000030004};
RX PubMed=25663028; DOI=10.1007/s10482-015-0398-2;
RA Lai Q., Li G., Liu X., Du Y., Sun F., Shao Z.;
RT "Pseudooceanicola atlanticus gen. nov. sp. nov., isolated from surface
RT seawater of the Atlantic Ocean and reclassification of Oceanicola
RT batsensis, Oceanicola marinus, Oceanicola nitratireducens, Oceanicola
RT nanhaiensis, Oceanicola antarcticus and Oceanicola flagellatus, as
RT Pseudooceanicola batsensis comb. nov., Pseudooceanicola marinus comb. nov.,
RT Pseudooceanicola nitratireducens comb. nov., Pseudooceanicola nanhaiensis
RT comb. nov., Pseudooceanicola antarcticus comb. nov., and Pseudooceanicola
RT flagellatus comb. nov.";
RL Antonie Van Leeuwenhoek 107:1065-1074(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 -!- 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:KGM47983.1}.
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DR EMBL; AQQX01000006; KGM47983.1; -; Genomic_DNA.
DR RefSeq; WP_043750909.1; NZ_AQQX01000006.1.
DR AlphaFoldDB; A0A0A0ED21; -.
DR STRING; 1461694.ATO9_15420; -.
DR eggNOG; COG1048; Bacteria.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000030004; 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:UP000030004}.
FT DOMAIN 83..593
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 723..848
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 409..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 924 AA; 100017 MW; 024A1B61233753CD CRC64;
MPITVGQDTS KTRKTLSVGS SSIAYYSIPA AEAAGLGEFS KLPAALKVVL ENMLRFEDGK
TVSVDDIKAF SDWGKSGGKN PVEIAYRPAR VLMQDFTGVP AVVDLAAMRD GIKGLGGDVQ
KINPLNPVDL VIDHSVMIDE FGNPRAFQMN VDREYERNME RYQFLKWGQG AFENFRVVPP
GTGICHQVNL EYLAKAVWTD KDQNGELVAY PDTLVGTDSH TTMVNGLAVL GWGVGGIEAE
AAMLGQPISM LIPEVVGFKL TGKMVEGTTG TDLVLKVVEM LREKGVVGKF VEFYGEGLDS
LPLADRATIA NMAPEYGATC GFFPIDDETL RYLRNTGRDD DTVALVEAYA KENGFWRSAD
YDPIYTDTLS LDMGTIVPAI SGPKRPQDYI ALDKASTEFA KFIKGLRDGK DATPAAEGRW
EAEGGAPEPR DIPGDEGNHK KGWYKDKDAA HQLHDGSIVI ASITSCTNTS NPYVMIGAGL
VARKARELGL NRKPWVKTSL APGSQVVSHY LEAAGLQEDL DAVGFNLVGY GCTTCIGNSG
PLAEPISKAI NDYDLVATSV LSGNRNFEGR ISPDVRANYL ASPPLVVAYA LVGDMNVDIA
NDPIGQDKNG NDVYLKDIWP SQAEIAELVE KTVTKEAFQS KYADVFKGDE KWQEVDTTDS
ETYDWPAAST YVQNPPYFQG MSKTPGTISN IEGAKVLAIL GDMVTTDHIS PAGSFKDTTP
AGKYLTDHQV PVREFNSYGS RRGNHEVMMR GTFANIRIKN EMLDGVEGGY TKGPDGEQTS
IYDAAMAYQE AGTPLVIFGG EQYGAGSSRD WAAKGTALLG VKAVIAENFE RIHRSNLVGM
GVIPFEFTGG DTRKTLGLKG DETVAISGLD TIKPLQEVPC TITYGDGSSK EIMIKCRIDT
AIEIEYIEHG GVLHYVLRDL AKAS
//
