ID A0A1I1CA32_9BACT Unreviewed; 743 AA.
AC A0A1I1CA32;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR009407};
DE EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR009407};
DE AltName: Full=Oxalosuccinate decarboxylase {ECO:0000256|PIRNR:PIRNR009407};
GN ORFNames=SAMN04489723_12251 {ECO:0000313|EMBL:SFB57610.1};
OS Algoriphagus aquimarinus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=237018 {ECO:0000313|EMBL:SFB57610.1, ECO:0000313|Proteomes:UP000198790};
RN [1] {ECO:0000313|EMBL:SFB57610.1, ECO:0000313|Proteomes:UP000198790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23399 {ECO:0000313|EMBL:SFB57610.1,
RC ECO:0000313|Proteomes:UP000198790};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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|PIRNR:PIRNR009407};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR009407-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR009407-3};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000256|PIRSR:PIRSR009407-3};
CC -!- SIMILARITY: Belongs to the monomeric-type IDH family.
CC {ECO:0000256|PIRNR:PIRNR009407}.
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DR EMBL; FOKK01000022; SFB57610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1CA32; -.
DR STRING; 237018.SAMN04489723_12251; -.
DR OrthoDB; 9807643at2; -.
DR Proteomes; UP000198790; Unassembled WGS sequence.
DR GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR InterPro; IPR004436; Isocitrate_DH_NADP_mono.
DR NCBIfam; TIGR00178; monomer_idh; 1.
DR PANTHER; PTHR36999; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR PANTHER; PTHR36999:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR Pfam; PF03971; IDH; 1.
DR PIRSF; PIRSF009407; IDH_monmr; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE 3: Inferred from homology;
KW Glyoxylate bypass {ECO:0000256|PIRNR:PIRNR009407};
KW Magnesium {ECO:0000256|PIRSR:PIRSR009407-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR009407-3};
KW NADP {ECO:0000256|PIRNR:PIRNR009407, ECO:0000256|PIRSR:PIRSR009407-4};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR009407};
KW Reference proteome {ECO:0000313|Proteomes:UP000198790};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT BINDING 84..89
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 134..141
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 137
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 352
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 549
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT BINDING 550
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 554
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT BINDING 586..587
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 591
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 602..604
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT BINDING 651
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT SITE 257
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT SITE 422
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ SEQUENCE 743 AA; 80541 MW; C86EB772986F67C1 CRC64;
MSNQTPKILY TLTDEAPALA TYSLLPIVEA FTKSAGVSVE TRDISLSARI ISNFSAFLTP
EQQMPDTLAE LGDIAKTPEA NIVKLPNISA SVPQLKAAIK ELQSQGYALP EYPEEPKTEE
EKSIKSKYDK IKGSAVNPVL REGNSDRRAP LAVKEYARKH PHSMGKWSAD SKTHVDSMTE
GDFYGSEKSH TMADAAIISI ELHGADGRKE ILKSGLNILA GEVIDASTLS ISALTAFLRK
AKAEAKLQGV LFSIHMKATM MKVSDPIIFG HAVKVFFEPV FAKHAATFNE VGIDVNNGFG
DLISNLDKLS IPKRTEVEAD IAACLADSPD LAMVNSDKGI TNLHVPSDVI IDASMPAMIR
TSGQMWNKAG KLQDTKAIIP DRSYAGVYEA TINFCKAHGA FDPSTMGSVP NVGLMAQKAE
EYGSHDKTFE VPFAGTVKVL DQNGIEIFSH NVEAGDIWRM CQTKDAPIQD WVKLAVTRAR
LSATPAIFWL DPNRAHDAEL IKKVNKYLLD HDQTGLEISI LSPIEATNLS LARIKEGMDT
ISVTGNVLRD YLTDLFPILE LGTSAKMLSI VPLMNGGGLF ETGAGGSAPK HVEQFVNEGH
LRWDSLGEFL ALAVSLEHLG QTFHNDKALL LGETLDQATG KWLENDKSPA RVVGKLDNRG
SHFYIALYWA EALAAQNKDA DLKAKFTVLA SALEAQETTI VNELNGSQGV PINIGGYFKP
NATLASEAMR PSATLNEVLT TLV
//
