ID A0A0B9AVE1_BRELN Unreviewed; 644 AA.
AC A0A0B9AVE1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Aconitate hydratase {ECO:0000313|EMBL:KHS53295.1};
GN ORFNames=AE0388_1238 {ECO:0000313|EMBL:KHS53295.1};
OS Brevibacterium linens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=1703 {ECO:0000313|EMBL:KHS53295.1, ECO:0000313|Proteomes:UP000031488};
RN [1] {ECO:0000313|EMBL:KHS53295.1, ECO:0000313|Proteomes:UP000031488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AE038-8 {ECO:0000313|EMBL:KHS53295.1,
RC ECO:0000313|Proteomes:UP000031488};
RA Maizel D., Utturkar S.M., Brown S.D., Ferrero M., Rosen B.P.;
RT "Draft Genome Sequence of Brevibacterium linens AE038-8.";
RL Submitted (NOV-2014) 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:KHS53295.1}.
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DR EMBL; JTJZ01000016; KHS53295.1; -; Genomic_DNA.
DR RefSeq; WP_039208060.1; NZ_JTJZ01000016.1.
DR AlphaFoldDB; A0A0B9AVE1; -.
DR STRING; 1703.BLSMQ_0714; -.
DR PATRIC; fig|1703.6.peg.1125; -.
DR OrthoDB; 9764318at2; -.
DR Proteomes; UP000031488; Unassembled WGS sequence.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
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; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR006250; Aconitase_put.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01342; acon_putative; 1.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 1.
DR Pfam; PF00330; Aconitase; 2.
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.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000031488}.
FT DOMAIN 10..285
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 288..407
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 517..579
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 644 AA; 69094 MW; C6007F154C4F4488 CRC64;
MAENVAQKLI RSHLESGELA PGNELGIRID QTLTQDATGT LVMLELEALG LDRIRTDLSV
QYVDHNLLQT DEKNPEDHEF LRSAAARFGL WFSPAGNGVS HPVHQSRFGK PGATLIGSDS
HTCAAGALGM LAIGVGGLEI AMAMAGEPLF ISAPQIMGVE LTGTLPDWVS AKDVILEMLR
RHGVKGGVGK IIEYHGDGLK NLTAMDRHVI ANMGAELGAT ATVFPADDAV RDYLEAVDRG
DDFTRLEADE GAEYDLTDSI DLSQLEPLIA APSSPGNVTP VREVAGDDVF QVVVGSSANP
GLRDFAVVAE ALSERQIHPQ ISLDINPTSR EVLADLIAGG WLTSLVGSGA RIHQSGCMGC
IGMGQAPAVG RNSLRTMPRN FPGRSGTDED SVWLCSPETA AAAALTGKIT DPRDLDMDYP
QVRLPEKYSA NRKMLVPPLG PEEARSVELV KGTNISTLPD FEPLPDDIDL EILLKVGDNV
STDEIMPAGS RVLPYRSNIP KISEFVYIQV DDTYATRAAE HEGGHAIVGG ENYGQGSSRE
HAVIAPRYLG LRVVVAKSLA RIHWQNLANF GVLALEFTDE ADYESLSQGD VLEFRGLRDE
LGEGTTITAE AAGRKFEFRH GLSPRQVEMV LAGGRIAQRA AHLN
//
