ID C0QL87_DESAH Unreviewed; 882 AA.
AC C0QL87;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
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:ACN14173.1};
GN OrderedLocusNames=HRM2_10610 {ECO:0000313|EMBL:ACN14173.1};
OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS HRM2) (Desulfobacterium autotrophicum).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulforapulum.
OX NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN14173.1, ECO:0000313|Proteomes:UP000000442};
RN [1] {ECO:0000313|EMBL:ACN14173.1, ECO:0000313|Proteomes:UP000000442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC {ECO:0000313|Proteomes:UP000000442};
RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA Meyerdierks A., Gottschalk G., Amann R.;
RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT reducer oxidizing organic carbon completely to carbon dioxide.";
RL Environ. Microbiol. 11:1038-1055(2009).
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; CP001087; ACN14173.1; -; Genomic_DNA.
DR RefSeq; WP_015902962.1; NC_012108.1.
DR AlphaFoldDB; C0QL87; -.
DR STRING; 177437.HRM2_10610; -.
DR KEGG; dat:HRM2_10610; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_7; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000000442; 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|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|RuleBase:RU361275, ECO:0000313|EMBL:ACN14173.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000442}.
FT DOMAIN 68..552
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 682..809
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 882 AA; 96949 MW; 61707B54131DF7E6 CRC64;
MKNRDYLKSF QVDGVRHTYF DFNQFAADRG ATLDKLPFSI KILVENLLRK LDNKVVNEND
LLNIVNWQKS YDTPVEIPYY PARVLMQDFT GVPAVVDLAA MRDAVKALGK DPASVNPKVP
TELIIDHSVQ VDNFGTQDCL EKNVALEYSR NGERYELLKW AQKSFSNFKV VPPNSGICHQ
VNLEHLGRVV ISDSEDGDSV VYPDTLVGTD SHTPMINGIG VMGWGVGGIE AEAVMLGQPY
YMSIPEVIGV KLVGRLKPGI TATDLVLTIT EMLRKVNVVE KFVEYFGPGM KSLSVTDRAT
IANMTPEYGA TLGFFPVDEK TLEYLEITGR KERAKIVEAY TKATGMFYTG ETTPDFTQVV
ELDLSTVELC VAGPARPQDR ICLPDLKERF QDSLASSKPQ FDMELNGQPI RIGDGSIVIA
AITSCTNTSN PHVLMGAGLI ARNAVARGLR VPPFVKTSLA PGSRVVMEYL ESAGLVPFFN
ALGFHVAGFG CTTCIGNSGP LHPEIEKIID TNELNVAAVL SGNRNFEARI HQKIKSNFLA
SPMLVVLFAL AGRVDIDLTT EPVGLDPNGE PVFMADLWPE FDEIDQLVKQ HVKQAFFEEK
YAHIFDGDQF WEALDIDQST TFAWNKTSTY IKNPPYFDGF SLNVQPPGDI RDARAFLVVG
DSVTTDHISP AGEIPEEYPA GKYLVEKGVA PEQFNSYGAR RGNHEVMMRG TFGNIRIKNE
LVAPKQGSFT LKFPEGKEMF NYDAAMAYAK EGTPLVVLGG KEYGTGSSRD WAAKGTALLG
IKAVIAGSYE RIHRNNLVGM GVLPLIFSNG DTAKSLGLDG RETYVISGVE KMTPGKTLSV
KAIKEDGSEI AFEVVSRLDT QVDVDYFENG GILPCVIRRM MV
//
