ID A8LNN2_DINSH Unreviewed; 357 AA.
AC A8LNN2;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=3-isopropylmalate dehydrogenase {ECO:0000313|EMBL:ABV95126.1};
DE EC=1.1.1.85 {ECO:0000313|EMBL:ABV95126.1};
GN Name=leuB {ECO:0000313|EMBL:ABV95126.1};
GN OrderedLocusNames=Dshi_3393 {ECO:0000313|EMBL:ABV95126.1};
OS Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Dinoroseobacter.
OX NCBI_TaxID=398580 {ECO:0000313|EMBL:ABV95126.1, ECO:0000313|Proteomes:UP000006833};
RN [1] {ECO:0000313|Proteomes:UP000006833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16493 / NCIMB 14021 / DFL 12
RC {ECO:0000313|Proteomes:UP000006833};
RX PubMed=19741735; DOI=10.1038/ismej.2009.94;
RA Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I.,
RA Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., Han C.,
RA Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., Liebl W.,
RA Liesegang H., Meincke L., Pati A., Petersen J., Piekarski T.,
RA Pommerenke C., Pradella S., Pukall R., Rabus R., Stackebrandt E., Thole S.,
RA Thompson L., Tielen P., Tomasch J., von Jan M., Wanphrut N., Wichels A.,
RA Zech H., Simon M.;
RT "The complete genome sequence of the algal symbiont Dinoroseobacter shibae:
RT a hitchhiker's guide to life in the sea.";
RL ISME J. 4:61-77(2010).
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};
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DR EMBL; CP000830; ABV95126.1; -; Genomic_DNA.
DR RefSeq; WP_012180052.1; NC_009952.1.
DR AlphaFoldDB; A8LNN2; -.
DR STRING; 398580.Dshi_3393; -.
DR KEGG; dsh:Dshi_3393; -.
DR eggNOG; COG0473; Bacteria.
DR HOGENOM; CLU_031953_0_1_5; -.
DR OrthoDB; 9767905at2; -.
DR Proteomes; UP000006833; Chromosome.
DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR PANTHER; PTHR43275; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 1.
DR PANTHER; PTHR43275:SF1; D-MALATE DEHYDROGENASE [DECARBOXYLATING]; 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 4: Predicted;
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Oxidoreductase {ECO:0000313|EMBL:ABV95126.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006833}.
FT DOMAIN 5..353
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
SQ SEQUENCE 357 AA; 37952 MW; E688BC73671CA927 CRC64;
MQSFSITVFD GDGIGPEIMA PTLGLLRKLA GTAATYDLNF DSHPMGAGHY AQTGQALPRA
SLDAARASDA ILLSAMGLPD IRYPDGTEIT PQIDIRIALD LYAGVRPVRI VPGHPTPLHA
PGPVDFVLIR ESTEGLFHTK GKGTVTKDHA TETLQITRDT SEKLFRFAFA LAAQRKASGR
GEGRVTCVDK ANVFRAFAFF REIFDAEAAR HPDLIADHAY VDAMALWMVT RPQTFDVMVT
ENMFGDILSD LGAGLMGGLG LAPSADIGDD NAVFQPCHGT APDIAGRGIA NPLAMILSAA
MMLDWLALRG QNAELATDGQ RLREAVEAVL TEGRVLTRDL GGNASTEEAA AAVAAKL
//