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Database: UniProt
Entry: A0A1Y4TJ95_9FIRM
LinkDB: A0A1Y4TJ95_9FIRM
Original site: A0A1Y4TJ95_9FIRM 
ID   A0A1Y4TJ95_9FIRM        Unreviewed;       372 AA.
AC   A0A1Y4TJ95;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=3-isopropylmalate dehydratase {ECO:0000313|EMBL:OUQ41200.1};
GN   ORFNames=B5E65_12995 {ECO:0000313|EMBL:OUQ41200.1};
OS   Gemmiger sp. An120.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Gemmiger.
OX   NCBI_TaxID=1965549 {ECO:0000313|EMBL:OUQ41200.1, ECO:0000313|Proteomes:UP000195783};
RN   [1] {ECO:0000313|Proteomes:UP000195783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An120 {ECO:0000313|Proteomes:UP000195783};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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:OUQ41200.1}.
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DR   EMBL; NFLN01000019; OUQ41200.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4TJ95; -.
DR   OrthoDB; 9764318at2; -.
DR   Proteomes; UP000195783; 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; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00330; Aconitase; 1.
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:UP000195783}.
FT   DOMAIN          51..206
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
SQ   SEQUENCE   372 AA;  39387 MW;  6C9249E0EEE84CB4 CRC64;
     MSTFVEKMLG APAGSPARIT PDLIVVNDGI CHTAVEMANL VRSPDKVRVI FDHDVPTGRP
     EAARVFGSIR RFARENNVRF IQAEGVGYQY LLEQEVRPGQ IVVQGGSHAG IYGSVGALGI
     NVSATELARV LEHDYYNTVV PETVAVRVEG TLPEHVTMMD AAMAFLSENP CLAGKAVEFC
     GPQLTAHQKA VLCSMACETG AFTAAVTDTE DQDLVLDLSR VVPMVTMPCS ARELQKDAVR
     QPLAVLAGMR LQAGQIGGYT GGTIEELRLA VSLIEGKTLA RGFRLTVAPA TSADFLKALD
     EGIIERFIDF GAQISAVGDH SVVTQGAGVI GKGEKLLTTG LYTYAGCMGV QDSEVYTGSV
     PSVMAAAVTG RL
//
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