(data stored in ACNUC7421 zone)

SWISSPROT: C8W662_DESAS

ID   C8W662_DESAS            Unreviewed;       523 AA.
AC   C8W662;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 81.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01032, ECO:0000256|HAMAP-Rule:MF_01033};
DE   Includes:
DE     RecName: Full=3-isopropylmalate dehydratase small subunit {ECO:0000256|HAMAP-Rule:MF_01032};
DE              EC=4.2.1.33 {ECO:0000256|HAMAP-Rule:MF_01032};
DE     AltName: Full=Alpha-IPM isomerase {ECO:0000256|HAMAP-Rule:MF_01032};
DE     AltName: Full=Isopropylmalate isomerase {ECO:0000256|HAMAP-Rule:MF_01032};
DE              Short=IPMI {ECO:0000256|HAMAP-Rule:MF_01032};
DE   Includes:
DE     RecName: Full=3-isopropylmalate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01033};
DE              EC=1.1.1.85 {ECO:0000256|HAMAP-Rule:MF_01033};
DE     AltName: Full=3-IPM-DH {ECO:0000256|HAMAP-Rule:MF_01033};
DE     AltName: Full=Beta-IPM dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01033};
DE              Short=IMDH {ECO:0000256|HAMAP-Rule:MF_01033};
GN   Name=leuB {ECO:0000256|HAMAP-Rule:MF_01033};
GN   Synonyms=leuD {ECO:0000256|HAMAP-Rule:MF_01032};
GN   OrderedLocusNames=Dtox_0597 {ECO:0000313|EMBL:ACV61517.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61517.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61517.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate
CC       and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
CC       {ECO:0000256|HAMAP-Rule:MF_01032}.
CC   -!- FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-
CC       methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-
CC       oxopentanoate. The product decarboxylates to 4-methyl-2
CC       oxopentanoate. {ECO:0000256|HAMAP-Rule:MF_01033,
CC       ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571560}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-
CC         oxopentanoate + CO2 + NADH; Xref=Rhea:RHEA:32271,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:17865, ChEBI:CHEBI:35121,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.85;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01033,
CC         ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS01118041};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate;
CC         Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121;
CC         EC=4.2.1.33; Evidence={ECO:0000256|HAMAP-Rule:MF_01032};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01033, ECO:0000256|RuleBase:RU004445};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01033, ECO:0000256|RuleBase:RU004445};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01033, ECO:0000256|RuleBase:RU004445};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00611795};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 2/4.
CC       {ECO:0000256|HAMAP-Rule:MF_01032}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-
CC       leucine from 3-methyl-2-oxobutanoate: step 3/4.
CC       {ECO:0000256|HAMAP-Rule:MF_01033, ECO:0000256|RuleBase:RU004445,
CC       ECO:0000256|SAAS:SAAS00571573}.
CC   -!- SUBUNIT: Heterodimer of LeuC and LeuD. {ECO:0000256|HAMAP-
CC       Rule:MF_01032}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01033,
CC       ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571561}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01033}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01033}.
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DR   EMBL; CP001720; ACV61517.1; -; Genomic_DNA.
DR   STRING; 485916.Dtox_0597; -.
DR   EnsemblBacteria; ACV61517; ACV61517; Dtox_0597.
DR   KEGG; dae:Dtox_0597; -.
DR   eggNOG; ENOG4105C0C; Bacteria.
DR   eggNOG; COG0066; LUCA.
DR   eggNOG; COG0473; LUCA.
DR   HOGENOM; HOG000021112; -.
DR   KO; K00052; -.
DR   OMA; DEWGYSE; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01577; IPMI_Swivel; 1.
DR   Gene3D; 3.20.19.10; -; 1.
DR   HAMAP; MF_01033; LeuB_type1; 1.
DR   HAMAP; MF_01032; LeuD_type2; 1.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   InterPro; IPR033940; IPMI_Swivel.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR   InterPro; IPR004429; Isopropylmalate_DH.
DR   InterPro; IPR011827; LeuD_type2/HacB/DmdB.
DR   PANTHER; PTHR42979; PTHR42979; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   SMART; SM01329; Iso_dh; 1.
DR   TIGRFAMs; TIGR00169; leuB; 1.
DR   TIGRFAMs; TIGR02087; LEUD_arch; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8W662.
DR   SWISS-2DPAGE; C8W662.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01033,
KW   ECO:0000256|SAAS:SAAS00571577};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
KW   Rule:MF_01033, ECO:0000256|RuleBase:RU004445,
KW   ECO:0000256|SAAS:SAAS00571571};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01033};
KW   Leucine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01033,
KW   ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571574};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01032,
KW   ECO:0000256|SAAS:SAAS00710129};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01033,
KW   ECO:0000256|SAAS:SAAS00571572};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01033,
KW   ECO:0000256|SAAS:SAAS00571566};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01033,
KW   ECO:0000256|RuleBase:RU004445, ECO:0000256|SAAS:SAAS00571558};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01033, ECO:0000256|RuleBase:RU004445,
KW   ECO:0000256|SAAS:SAAS00571565};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01033,
KW   ECO:0000256|SAAS:SAAS00571564};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT   DOMAIN      169    516       Iso_dh. {ECO:0000259|SMART:SM01329}.
FT   METAL       389    389       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   METAL       413    413       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   METAL       417    417       Magnesium or manganese.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   BINDING     262    262       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   BINDING     272    272       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   BINDING     300    300       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   BINDING     389    389       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01033}.
FT   SITE        307    307       Important for catalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
FT   SITE        357    357       Important for catalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_01033}.
SQ   SEQUENCE   523 AA;  56813 MW;  3A6884E2350A6254 CRC64;
     MGLKGKAWKF GADIDTDAII PARYLNTSDP VELAKHCMED ADTSFAQKVQ PGDVIVADKN
     FGCGSSREHA PISIKYAGVS CVIAKSFARI FYRNAFNIGL PILESTEAVE GIDEGNEVSV
     NAETGTITNV TKGETYQATV VPPFMQQIIA AGGLINYVAE RMKVKKMYKI AVLPGDGIGP
     EITEQALKAL KAVAEHFGHE FQFTEALVGG AAYDAVGHPL PKETLDLCYS SDAILLGAVG
     GDKWADLPPE LTPERGALLP LRKLLGLYAN LRPAVVFPAL ANASTLKPEV VEGLDIMVVR
     ELTGGLYFGE KKREDLPDGT VRVTDTLVYT TEEIVRIARL AFELAAKRRK KVTLVDKANV
     LESSRYWREV VANMAAEYPD IEFNTMYVDN AAMQLVKMPK QFDVIVTDNM FGDILSDQAS
     QLTGSLGMLA SASIGGKIGL YEPSHGSAPK YAGLKRANPI ATVMSGAMLL RYSFDMEKEA
     KAIEDAVTEV LKKYRTRDIM EEGLQLVNTD EMGDRIAEQI LAG
//

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