ID A0A0Q8R6U9_9SPHN Unreviewed; 442 AA.
AC A0A0Q8R6U9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Homoaconitate hydratase {ECO:0000256|ARBA:ARBA00032706};
GN ORFNames=ASE22_13735 {ECO:0000313|EMBL:KRB91290.1};
OS Sphingomonas sp. Root720.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736595 {ECO:0000313|EMBL:KRB91290.1, ECO:0000313|Proteomes:UP000051570};
RN [1] {ECO:0000313|Proteomes:UP000051570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root720 {ECO:0000313|Proteomes:UP000051570};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB91290.1, ECO:0000313|Proteomes:UP000051570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root720 {ECO:0000313|EMBL:KRB91290.1,
RC ECO:0000313|Proteomes:UP000051570};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRB91290.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMID01000011; KRB91290.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q8R6U9; -.
DR STRING; 1736595.ASE22_13735; -.
DR Proteomes; UP000051570; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0043436; P:oxoacid metabolic process; IEA:UniProt.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR PANTHER; PTHR43822:SF25; HOMOACONITASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00330; Aconitase; 2.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000051570}.
FT DOMAIN 91..294
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 300..423
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
SQ SEQUENCE 442 AA; 46937 MW; AC045B88AF938FAB CRC64;
MAGAPQEGER VMGSTMAAKI LARAAGIERA ETGAAVLAKV SLMTCLDGTT FIDTFRKRNL
KVWDPSRLIF CFDHFFQPEW FPQQAGKEHP KIKSFAKEQG VPAENIYDVG RNGISHHIPV
EQGWALPGAV CIGADTQSST MGAANCFALP ALWGVDPIIL TGDIWMIVPQ CVRINLTGSL
PQGLNGKDVV YRLIDDLSET VGGKVLEFSG PGVASLPMDF RLAIANGAVQ IGALTIVFPH
DEVLADYLDG RAREGFEPVA ADDDADYVAT YDYDLSSFDT LVAGPHDIEL VRPLGNVLGL
EVTAANIGSC SSGRLSDLRL AAEVLRDRKV HPAVRLVVTP ISADTHREAA HAGLLEVFLD
AGATVTQPGC GACYSGNLSP LKLGDGERCI STSVETLRGR MGSQESEVML ANAAVVAASA
IEGRIADPAP YLARAMEASH EA
//
