ID A0A0S3F4P4_9SPHN Unreviewed; 889 AA.
AC A0A0S3F4P4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=ATN00_10810 {ECO:0000313|EMBL:ALR22546.1};
OS Sphingobium baderi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1332080 {ECO:0000313|EMBL:ALR22546.1, ECO:0000313|Proteomes:UP000056968};
RN [1] {ECO:0000313|EMBL:ALR22546.1, ECO:0000313|Proteomes:UP000056968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DE-13 {ECO:0000313|EMBL:ALR22546.1,
RC ECO:0000313|Proteomes:UP000056968};
RA Cheng M., Meng Q., Yang Y., Chu C., Yan X., He J., Li S.;
RT "A Two-component Flavoprotein Monooxygenase System MeaXY Responsible for
RT para-Hydroxylation of 2-Methyl-6-ethylaniline and 2,6-Diethylaniline in
RT Sphingobium baderi DE-13.";
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}.
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DR EMBL; CP013264; ALR22546.1; -; Genomic_DNA.
DR RefSeq; WP_062068683.1; NZ_CP013264.1.
DR AlphaFoldDB; A0A0S3F4P4; -.
DR STRING; 1332080.ATN00_10810; -.
DR KEGG; sbd:ATN00_10810; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000056968; 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:UP000056968}.
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; 95788 MW; 0FC4D7331DA68369 CRC64;
MTAIGQDTLG TRDTLKVGGK DIAYYSLKKA AARLGDVSRL PFSMKVLLEN LLRFEDGVTV
TVEDIQAIVD WQKDRRSERE IQYRPARVLM QDFTGVPCVV DLAAMRDAMN NLGADASKIN
PQVPVHLVID HSVMVDEFGT PQAFEDNVEL EYQRNMERYD FLKWGSKSLN NFKVVPPGTG
ICHQVNLENI AQAVWSSVDA DGNIVAYPDT CVGTDSHTTM INGLGVLGWG VGGIEAEAAM
LGQPVSMLIP EVVGFKLTGT LGEGITATDL VLTATQMLRA KGVVGRFVEY FGPGLASLSL
ADRATLANMA PEYGATCGFF GIDDKTLDYM RLTGRSEENI ALVEAYAKEQ GFWLDASVDP
VFTDILELDM STVVPSLAGP KRPQDKVILT QVDNVFNADL EKLYKKAAPA RVAVEGRTHD
IGDGDVVIAA ITSCTNTSNP GVLVAAGLVA KKAVEKGLKP KPWVKTSLAP GSQVVTDYLE
KAGLQSYLDQ VGFNLVGYGC TTCIGNSGPL AEPISKAING NDIVAASVLS GNRNFEGRVS
PDVRANFLAS PPLVVAYALK GTVTTDFVAT PIGQGSDGQD VYLKDIWPTN DEVRSVMDGA
LTRNMFESRY ATVFTGDARW QAINVTGSDT YSWRAGSTYV ANPPYFEGLT MTPAPVTDIV
DAKPLAIFGD SITTDHISPA GSIKASSPAG KWLSEHQVAQ ADFNSYGARR GHHEVMMRGT
FANIRIKNLM LDGVEGGMTR YEGEIMPIYD AAMKHKADGT PLVVIGGKEY GTGSSRDWAA
KGTNLLGVRS VIVESFERIH RSNLVGMGVL PLQFKDGQNK DTLGLTGDET FTITGVAGLK
PRQDVDVKVT RADGSTFTFT ALCRIDTVNE LDYFLNGGIL QYVLRKLAA
//
