ID Q28NZ9_JANSC Unreviewed; 931 AA.
AC Q28NZ9;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 115.
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 OrderedLocusNames=Jann_2646 {ECO:0000313|EMBL:ABD55563.1};
OS Jannaschia sp. (strain CCS1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=290400 {ECO:0000313|EMBL:ABD55563.1, ECO:0000313|Proteomes:UP000008326};
RN [1] {ECO:0000313|Proteomes:UP000008326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS1 {ECO:0000313|Proteomes:UP000008326};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W.,
RA Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABD55563.1, ECO:0000313|Proteomes:UP000008326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS1 {ECO:0000313|EMBL:ABD55563.1,
RC ECO:0000313|Proteomes:UP000008326};
RX PubMed=17526795; DOI=10.1128/AEM.02580-06;
RA Moran M.A., Belas R., Schell M.A., Gonzalez J.M., Sun F., Sun S.,
RA Binder B.J., Edmonds J., Ye W., Orcutt B., Howard E.C., Meile C.,
RA Palefsky W., Goesmann A., Ren Q., Paulsen I., Ulrich L.E., Thompson L.S.,
RA Saunders E., Buchan A.;
RT "Ecological genomics of marine Roseobacters.";
RL Appl. Environ. Microbiol. 73:4559-4569(2007).
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; CP000264; ABD55563.1; -; Genomic_DNA.
DR RefSeq; WP_011455767.1; NC_007802.1.
DR AlphaFoldDB; Q28NZ9; -.
DR STRING; 290400.Jann_2646; -.
DR KEGG; jan:Jann_2646; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_5; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000008326; 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|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:UP000008326}.
FT DOMAIN 82..594
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 725..849
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 421..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 931 AA; 100786 MW; 080DAA59DD10D79C CRC64;
MPITVGHDTS KTRKTLTVGG QSVAYYSIAA AEAAGLGDFS KLPAALKVVL ENMLRFEDGT
TVSVDDIKAF SDWAAKGGKN PREIAYRPAR VLMQDFTGVP AVVDLAAMRD GIKALGGDPQ
KINPLNPVDL VIDHSVMIDE FGNPRAFQMN VDREYERNME RYTFLKWGQT AFNNFRVVPP
GTGICHQVNL EYLAQTVWTD TDQNGDEVAY PDTLVGTDSH TTMVNGAAVL GWGVGGIEAE
AAMLGQPISM LIPEVVGFEL TGAMMEGTTG TDLVLKVVEL LRERGVVGKF VEFYGKGLDS
LPLADRATIA NMAPEYGATC GFFPIDGETL RYLRTTGRDE DRIALVEAYA KENGFWRGDD
YVPVYTDTLH LDMGTIVPAI SGPKRPQDYI ALDKAAATFH EYVVGQRSAK DAGAKQEIKW
EGEGGAPEPT DIPGDAGSHA RGYVDNPDGE NYQLHDGSIV IASITSCTNT SNPYVMIGAG
LVARKAHALG LTRKPWVKTS LAPGSQVVSA YLEAAELQDD LDAIGFNLVG YGCTTCIGNS
GPLQEEISKA INDNDLIGVS VLSGNRNFEG RISPDVRANY LASPPLVVAY ALIGDMNVDI
TTASLGTDKD GNDVYLKDIW PSTQEIAELV EETVTRESFQ EKYADVFKGD DKWQGVEITD
AEVYDWPATS TYIQNPPYFQ GMTMDTKKIE NIEDAKVLAV LGDFITTDHI SPAGSFKESH
PAGQYLVERQ VPVREFNSYG SRRGNHEVMM RGTFANIRIK NEMLDGVEGG YTLGPDGEQT
SIFDAAMAYQ EQGTPLVIFG GEQYGAGSSR DWAAKGTNLL GVKAVIAESF ERIHRSNLVG
MGVIPFEFTG GDTRKSLGLK GDETVSIHGL DAVTPLAEVP ATITMGDGSV KEITLKCRID
TGVEIEYIEN GGVLHYVLRN LARDDQPIAA E
//
