ID A0A0W1QMK2_9SPHN Unreviewed; 890 AA.
AC A0A0W1QMK2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=ATB93_08875 {ECO:0000313|EMBL:KTF69461.1};
OS Sphingomonas sp. WG.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1592629 {ECO:0000313|EMBL:KTF69461.1, ECO:0000313|Proteomes:UP000052965};
RN [1] {ECO:0000313|EMBL:KTF69461.1, ECO:0000313|Proteomes:UP000052965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WG {ECO:0000313|EMBL:KTF69461.1,
RC ECO:0000313|Proteomes:UP000052965};
RA Li H., Feng Z., Sun Y., Jiao X., Zhou W., Zhu H.;
RT "Draft Genome Sequence of Sphingomonas sp. WG, a welan gum producing
RT strain.";
RL Submitted (NOV-2015) 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:KTF69461.1}.
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DR EMBL; LNOS01000032; KTF69461.1; -; Genomic_DNA.
DR RefSeq; WP_019369762.1; NZ_LNOS01000032.1.
DR AlphaFoldDB; A0A0W1QMK2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000052965; 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:UP000052965}.
FT DOMAIN 71..563
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 692..817
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 890 AA; 95882 MW; 170DF3AE71A74187 CRC64;
MTAIGNDTLG TRDSLTVSGK TYSFYSLPKA AEKLGDISRL PFSMKVLLEN MLRFDDGVTV
TPEDAQAIVD WQKNPKAPSR EIQYRPARVL MQDFTGVPCV VDLAAMRDAI TKLGGDAAKI
NPLVPVHLVI DHSVMVDEFG TPQAFDDNVK LEYERNAERY EFLKWGSKAL NNFSVVPPGT
GICHQVNLEY IAQSIWSSVA PDGATIAYPD TLVGTDSHTT MVNGLGVLGW GVGGIEAEAA
MLGQPVSMLI PEVVGFKLTG ALPEGITATD LVLTVTQMLR AKGVVGRFVE FYGPGLHSMT
LADRATIANM APEYGATCGF FPIDDKTLDY MRLTGRPDET VALVEAYAKA QGMWHDVGGP
EPVFTDTLEL DMSTVRPSLA GPKRPQDRVS LDSVDEVFNG DLTKVYKKEQ PARVSVEGRD
HDIGDGDVVI AAITSCTNTS NPSVLIAAGL VARKARALGL TRKPWVKTSL APGSQVVTDY
LNKAGLSEDL DAIGFNLVGY GCTTCIGNSG PLAEPISQAI NGNDIVAASV LSGNRNFEGR
VSPDVRANFL ASPPLVVAYA LKGTVTEDMY ETPIGEGTNG PVFLKDIWPS NEEIQGLIAA
NIDDDMFRSR YGNVYLGDRH WQGITVTGSD TYSWPTSSTY IHNPPYFEGM SMTPAPVQDI
VDAKPLAILG DSITTDHISP AGSIKADSPA GAFLQSHQVA KKDFNSYGAR RGNDEVMVRG
TFANIRIKNE MVPGVEGGMT KYAGEVMPIY DAAMRHKADG TALVIVAGKE YGTGSSRDWA
AKGTNLLGVR AVITESFERI HRSNLVGMGV LPLQFAEGVT RETLKLDGTE TFTITGVAGL
RPRQDVEVKL TRADGSSETF LTRCRIDTVN ELEYFLNGGI LHYVLRKLAA
//
