ID S9RDQ8_9RHOB Unreviewed; 924 AA.
AC S9RDQ8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=Salmuc_01251 {ECO:0000313|EMBL:EPX76265.1};
OS Salipiger mucosus DSM 16094.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1123237 {ECO:0000313|EMBL:EPX76265.1, ECO:0000313|Proteomes:UP000015347};
RN [1] {ECO:0000313|Proteomes:UP000015347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16094 {ECO:0000313|Proteomes:UP000015347};
RX PubMed=25197501; DOI=10.4056/sigs.4909790;
RA Riedel T., Spring S., Fiebig A., Petersen J., Kyrpides N.C., Goker M.,
RA Klenk H.P.;
RT "Genome sequence of the exopolysaccharide-producing Salipiger mucosus type
RT strain (DSM 16094(T)), a moderately halophilic member of the Roseobacter
RT clade.";
RL Stand. Genomic Sci. 9:1331-1343(2014).
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:EPX76265.1}.
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DR EMBL; APVH01000056; EPX76265.1; -; Genomic_DNA.
DR RefSeq; WP_020041921.1; NZ_KE557284.1.
DR AlphaFoldDB; S9RDQ8; -.
DR STRING; 1123237.Salmuc_01251; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_5; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000015347; 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:UP000015347}.
FT DOMAIN 81..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"
SQ SEQUENCE 924 AA; 100489 MW; 2A3C8DB40311A637 CRC64;
MPITVGQDTA KARKSLEVNG KTYAYYSIPA AEAAGLGDFS KLPAALKVVL ENMLRFEDGK
TVSVDDIKAF SDWAKNGGKG DRELAYRPAR VLMQDFTGVP AVVDLAAMRD GIKALGGDAQ
KINPLNPVDL VIDHSVMIDE FGNPRAFQMN VDREYERNIE RYEFLKWGQG AFNNFRVVPP
GTGICHQVNL EYLAQTVWTD EDQNGEAVAY PDTLVGTDSH TTMVNGAAVL GWGVGGIEAE
AAMLGQPISM LIPEVVGFEL TGKMLEGTTG TDLVLKVVEM LREKGVVGKF VEFYGDGLDN
LPLADRATIA NMAPEYGATC GFFPIDAETL RYLEMTGRDK DRIALVEAYA KENGFWRDGS
YNPVYTDTLS LDMGTIVPAI SGPKRPQDYI ALDKAAGAFG EYIKGVRNGE KVSENAEVRW
EAEGGAPEPV DIPGDQGHHK RGFAQTGEHK YQLHDGSVVI ASITSCTNTS NPYVMIGAGL
VARKARELGL DRKPWVKTSL APGSQVVSAY LEEAGLQEDL DAVGFNLVGY GCTTCIGNSG
PLADEISKCI NDNDLVATSV LSGNRNFEGR ISPDVRANYL ASPPLVVIYA LAGDMNIDVA
NDPIAQTPDG KDVYLKDLWP TQQEIADLVE KTVTRESFQE KYADVFKGDE KWQAVETTDA
ETYSWPASST YVQNPPYFQG MSKDPGTISN IEGARVLAVL GDMITTDHIS PAGSFKESTP
AGQYLREHQV PVREFNSYGS RRGNHEVMMR GTFANIRIKN EMLNGTEGGY TLDPNGNETS
IYEAAMAYQD QGTPLVVFGG ELYGAGSSRD WAAKGTALLG VKAVIAESFE RIHRSNLVGM
GVIPFEFTGD DDRETLKLTG KETVSIHGLE DVKPGQMTPC TITYEDGSTK DIELKCRIDT
AIEREYVEHG GVLHYVLRNL AKAA
//
