ID A4A3B8_9GAMM Unreviewed; 417 AA.
AC A4A3B8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|RuleBase:RU004446};
DE EC=1.1.1.42 {ECO:0000256|RuleBase:RU004446};
GN ORFNames=KT71_16016 {ECO:0000313|EMBL:EAQ99191.1};
OS Congregibacter litoralis KT71.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Congregibacter.
OX NCBI_TaxID=314285 {ECO:0000313|EMBL:EAQ99191.1, ECO:0000313|Proteomes:UP000019205};
RN [1] {ECO:0000313|EMBL:EAQ99191.1, ECO:0000313|Proteomes:UP000019205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT71 {ECO:0000313|EMBL:EAQ99191.1,
RC ECO:0000313|Proteomes:UP000019205};
RX PubMed=17299055; DOI=10.1073/pnas.0608046104;
RA Fuchs B.M., Spring S., Teeling H., Quast C., Wulf J., Schattenhofer M.,
RA Yan S., Ferriera S., Johnson J., Glockner F.O., Amann R.;
RT "Characterization of a marine gammaproteobacterium capable of aerobic
RT anoxygenic photosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2891-2896(2007).
RN [2] {ECO:0000313|EMBL:EAQ99191.1, ECO:0000313|Proteomes:UP000019205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT71 {ECO:0000313|EMBL:EAQ99191.1,
RC ECO:0000313|Proteomes:UP000019205};
RX PubMed=19287491; DOI=10.1371/journal.pone.0004866;
RA Spring S., Lunsdorf H., Fuchs B.M., Tindall B.J.;
RT "The photosynthetic apparatus and its regulation in the aerobic
RT gammaproteobacterium Congregibacter litoralis gen. nov., sp. nov.";
RL PLoS ONE 4:E4866-E4866(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH;
CC Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42;
CC Evidence={ECO:0000256|ARBA:ARBA00023554};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR604439-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR604439-3};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000256|PIRSR:PIRSR604439-3};
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}.
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:EAQ99191.1}.
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DR EMBL; AAOA02000001; EAQ99191.1; -; Genomic_DNA.
DR RefSeq; WP_008295638.1; NZ_CM002299.1.
DR AlphaFoldDB; A4A3B8; -.
DR SMR; A4A3B8; -.
DR STRING; 314285.KT71_16016; -.
DR eggNOG; COG0538; Bacteria.
DR HOGENOM; CLU_031953_7_1_6; -.
DR OrthoDB; 9806254at2; -.
DR Proteomes; UP000019205; Chromosome.
DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR004439; Isocitrate_DH_NADP_dimer_prok.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR NCBIfam; TIGR00183; prok_nadp_idh; 1.
DR PANTHER; PTHR43504; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR PANTHER; PTHR43504:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 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 Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435,
KW ECO:0000256|RuleBase:RU004446};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR604439-3};
KW Manganese {ECO:0000256|PIRSR:PIRSR604439-3, ECO:0000256|RuleBase:RU004446};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004446};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRSR:PIRSR604439-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EAQ99191.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019205};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU004446}.
FT DOMAIN 30..413
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 105
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-3"
FT BINDING 340..346
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 353
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 392
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT BINDING 396
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT SITE 161
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT SITE 231
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT MOD_RES 101
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT MOD_RES 143
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
SQ SEQUENCE 417 AA; 45292 MW; CF5683E887776A33 CRC64;
MGYQHIKVPD SGTRITVNDD NSLNVPDNPI IPYIEGDGIG VDISPVMIDV VDAAVAKAYD
GKKKISWMEI YTGEKAAELY EGDWFPEETL EAIKEYSVGI KGPLTTPVGG GFRSLNVALR
QELDLYTCLR PVRWFEGVPS PVKAPGDCNM VIFRENSEDI YAGIEYEAGT DEAKKVVDFI
IKEMGATKIR FPTNVGIGIK PVSEEGTKRL VRKAIQYAID QDLPSVTLVH KGNIMKFTEG
AFRDWGYELA QEEFGGELLD GGPWVSVKNP NTGKEIIIKD VIADAMLQQI LTRPKDYSVV
ATLNLNGDYL SDALAAQVGG IGIAPGANLS DKIALFEATH GTAPKYAGQD KVNPGSLILS
AEMMLRHMGW NEAADLIIDG MNGAIQNGTV TYDFERLMEG ATLVSCSGFG EKIIAAM
//
