ID A0A086PFE9_SPHHM Unreviewed; 889 AA.
AC A0A086PFE9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=BV98_000369 {ECO:0000313|EMBL:KFG92117.1};
OS Sphingobium herbicidovorans (strain ATCC 700291 / DSM 11019 / NBRC 16415 /
OS MH) (Sphingomonas herbicidovorans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1219045 {ECO:0000313|EMBL:KFG92117.1, ECO:0000313|Proteomes:UP000024284};
RN [1] {ECO:0000313|EMBL:KFG92117.1, ECO:0000313|Proteomes:UP000024284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16415 {ECO:0000313|EMBL:KFG92117.1,
RC ECO:0000313|Proteomes:UP000024284};
RA Gan H.M., Gan H.Y., Savka M.A.;
RT "Draft genome sequences of Sphingobium herbicidovorans.";
RL Submitted (AUG-2014) 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:KFG92117.1}.
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DR EMBL; JFZA02000001; KFG92117.1; -; Genomic_DNA.
DR RefSeq; WP_037462093.1; NZ_JFZA02000001.1.
DR AlphaFoldDB; A0A086PFE9; -.
DR STRING; 76947.GCA_002080435_00649; -.
DR PATRIC; fig|1219045.3.peg.373; -.
DR eggNOG; COG1048; Bacteria.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000024284; 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:UP000024284}.
FT DOMAIN 71..561
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 693..816
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 889 AA; 95675 MW; C2393BB93D26E8AD CRC64;
MTAIGQDTLG TRDTLNVGGK DIAYYSLKKA AAKLGDVSRL PFSMKVLLEN LLRFEDGVTV
TTDDIKAIVD WQNDKGKAER EIQYRPARVL MQDFTGVPCV VDLAAMRDAM TALGADASKI
NPQVPVHLVI DHSVMVDEFG TPKAFEQNVE IEYQRNMERY DFLKWGSKSL ANFYAVPPGT
GICHQVNLEN IAQAVWSSEG PDGVTVAYPD TCVGTDSHTT MINGLGVLGW GVGGIEAEAA
MLGQPVSMLI PEVVGFKLTG ELKEGVTATD LVLTATQMLR AKGVVGRFVE YFGPGLASLS
LADRATLANM APEYGATCGF FGIDDKTLDY MRLTGRSDEN IALVEAYAKE QGFWIDPSVE
PVFTDTLELD LATVVPSLAG PKRPQDRVSL PEVDDVFNAD MANVYKKAQQ RVPVEGKDFD
IGDGDVTIAA ITSCTNTSNP GVMVAAGLVA KKANELGLKP KPWVKTSLAP GSQVVTDYFA
KAGLQEHLDA VGFNLVGYGC TTCIGNSGPL AEPISKAINE NGLVAAAVIS GNRNFEGRVS
PDVRANFLAS PPLVVAYALK GTVIEDFITT PIGKGKDGQD VYLKDIWPTN DEVATTMAGC
MDRAMFQARY ANVYKGDAHW QAIDVTGSAT YAWRAGSTYV ANPPYFEGLS MTPAPVNDII
EAKPLAVFGD SITTDHISPA GSIKATSPAG KWLSEHQVAQ ADFNSYGARR GHHEVMMRGT
FANIRIKNLM LDGVEGGMTR YNGEIMPIYD AAMKHKADGT PLVVIGGKEY GTGSSRDWAA
KGTNLLGVRA VIVESFERIH RSNLVGMGVL PLQFKNGESK DTLGLTGDET FTIQNVSGLK
PRQDVEVLVK RADGSTFTFT ALCRIDTVNE LDYFLNGGIL QYVLRKLAA
//
