ID A0A0X8G4K8_9FIRM Unreviewed; 334 AA.
AC A0A0X8G4K8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Isocitrate dehydrogenase {ECO:0000313|EMBL:AMC09563.1};
GN ORFNames=AT726_12015 {ECO:0000313|EMBL:AMC09563.1};
OS Turicibacter sp. H121.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Turicibacteraceae; Turicibacter.
OX NCBI_TaxID=1712675 {ECO:0000313|EMBL:AMC09563.1, ECO:0000313|Proteomes:UP000057144};
RN [1] {ECO:0000313|Proteomes:UP000057144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H121 {ECO:0000313|Proteomes:UP000057144};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMC09563.1, ECO:0000313|Proteomes:UP000057144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H121 {ECO:0000313|EMBL:AMC09563.1,
RC ECO:0000313|Proteomes:UP000057144};
RX PubMed=27013036;
RA Auchtung T.A., Holder M.E., Gesell J.R., Ajami N.J., Duarte R.T., Itoh K.,
RA Caspi R.R., Petrosino J.F., Horai R., Zarate-Blades C.R.;
RT "Complete Genome Sequence of Turicibacter sp. Strain H121, Isolated from
RT the Feces of a Contaminated Germ-Free Mouse.";
RL Genome Announc. 4:0-0(2016).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000256|ARBA:ARBA00007769}.
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DR EMBL; CP013476; AMC09563.1; -; Genomic_DNA.
DR RefSeq; WP_068759683.1; NZ_JAMQUX010000020.1.
DR AlphaFoldDB; A0A0X8G4K8; -.
DR STRING; 1712675.AT726_12015; -.
DR KEGG; tur:AT726_12015; -.
DR OrthoDB; 9806254at2; -.
DR Proteomes; UP000057144; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004434; Isocitrate_DH_NAD.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR NCBIfam; TIGR00175; mito_nad_idh; 1.
DR PANTHER; PTHR11835; DECARBOXYLATING DEHYDROGENASES-ISOCITRATE, ISOPROPYLMALATE, TARTRATE; 1.
DR PANTHER; PTHR11835:SF34; ISOCITRATE DEHYDROGENASE [NAD] SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000057144};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 3..327
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 334 AA; 36308 MW; DE853D51991E2503 CRC64;
MRTVTLIPGD GIGPEISQSV VKIFEAAKVP IKFEIVEAGA KVMDQEKTPL PQAVLDSIQK
NKVALKGPIT TPIGSGFRSV NVALRQYFDL YANVRPVKSI KGVPSRYEEV DLIIVRENTE
DLYAGIEHKI GDVAAESIKV ITKKASDRIA TYAFTLANQQ QREKVTAVHK ANIMKLSDGL
FLECVRDIRK QYPDIEYDEQ IVDAMCMNLV LHPESSDVLV MGNLYGDILS DLCAGFVGGL
GLIPGANIGE EIAIFEAVHG SAPSIAGCNQ ANPTALIQSA IMMLRHLNLL NEANRIEAAL
YAVYEQGQDL TKDLGGTATT TQFTDALIAK LLNH
//
