ID A0A2A3VIE1_9GAMM Unreviewed; 921 AA.
AC A0A2A3VIE1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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:PBS11901.1};
GN ORFNames=CMZ82_12235 {ECO:0000313|EMBL:PBS11901.1};
OS Xanthomonadaceae bacterium NML93-0792.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae.
OX NCBI_TaxID=2032566 {ECO:0000313|EMBL:PBS11901.1, ECO:0000313|Proteomes:UP000218683};
RN [1] {ECO:0000313|EMBL:PBS11901.1, ECO:0000313|Proteomes:UP000218683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML93-0792 {ECO:0000313|EMBL:PBS11901.1,
RC ECO:0000313|Proteomes:UP000218683};
RA Bernier A.-M., Bernard K.;
RT "Clinical and environmental strains of Xanthomonadaceae.";
RL Submitted (SEP-2017) 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:PBS11901.1}.
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DR EMBL; NTJH01000015; PBS11901.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3VIE1; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000218683; 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}.
FT DOMAIN 66..586
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 716..845
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 396..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 921 AA; 99550 MW; 6AD7694E8638126F CRC64;
MTDSFSTHAE LDVGGRRLAY ASLPALGSRF DIARLPYSLK ILLENLLRHE DGESVTARHI
EAVATWDPKA QPDTEIAFMP ARVVLQDFTG VPCVVDLAAM RDAVVKLGGR PEQINPQIPS
ELVIDHSVQV DVFGRPDALD LNGKIEFERN KERYGFLRWG QKAFDNFKVV PPNTGIVHQV
NLEHLARVVM TSEREDGTVW AYPDTVFGTD SHTTMINGIG VLGWGVGGIE AEAAMLGQPS
SMLIPQVVGF KLKGRLPEGA TATDLVLTVT EMLRKHGVVG KFVEFFGDGL QHLPLADRAT
IGNMAPEYGA TCGIFPIDAE SLNYLRLSGR SEEQIALVEA YAKAQQLWHE PGAPEAEYSS
VLELDMADVR PSLAGPKRPQ DRVLLEKVQQ NFRDNVGPLT AKRDAASSED PQVDRFEKEG
GGQPQAERLA ARPVSKITLE DGEHELTDGS VVIAAITSCT NTSNPAVMLG AGLLARNAAA
KGLKAAPWVK TSLGPGSLVV TDYLKKAGVM DDLEALGFYV VGYGCTTCIG NSGPLPDAVS
KGIAENDLAV ASVLSGNRNF EGRIHGEVKM NYLASPPLVV AYAIAGTVDI DLTQDPLGKD
PDGNPVYLRD IWPTNQEIGD FIAKTIGPEM FAKNYADVFK GDTRWNTIDS PDGDLYEWDA
ASTYIKNPPY FEGMTMDVGS IDDIHGARVM GLFGDSITTD HISPAGNIKK DSPAGRFLQD
RGVQPADFNS YGSRRGNDDV MVRGTFANIR IKNLFFGGEE GGNTLYFGKG EPEKLAIYDA
AQKYKADGVP LVVFAGKEYG TGSSRDWAAK GTNLLGIKAV IAESFERIHR SNLVGMGVLP
CQFKAGENAQ THGLDGSETI DITGLDDGKA RTARVKATRG SGETVEFDVD VLLLTPKEVE
YFRHGGLLHY VLRQLAAKKA A
//
