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Database: UniProt
Entry: A0A167HCF8_9FLAO
LinkDB: A0A167HCF8_9FLAO
Original site: A0A167HCF8_9FLAO 
ID   A0A167HCF8_9FLAO        Unreviewed;       742 AA.
AC   A0A167HCF8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=ULVI_07720 {ECO:0000313|EMBL:OAB78475.1};
OS   Cochleicola gelatinilyticus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Cochleicola.
OX   NCBI_TaxID=1763537 {ECO:0000313|EMBL:OAB78475.1, ECO:0000313|Proteomes:UP000077013};
RN   [1] {ECO:0000313|EMBL:OAB78475.1, ECO:0000313|Proteomes:UP000077013}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0005 {ECO:0000313|EMBL:OAB78475.1,
RC   ECO:0000313|Proteomes:UP000077013};
RA   Shin S.-K., Yi H.;
RT   "Ulvibacter sp. LPB0005, isolated from Thais luteostoma.";
RL   Submitted (FEB-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}.
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:OAB78475.1}.
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DR   EMBL; LRXL01000037; OAB78475.1; -; Genomic_DNA.
DR   RefSeq; WP_068591493.1; NZ_LRXL01000037.1.
DR   AlphaFoldDB; A0A167HCF8; -.
DR   STRING; 1763537.ULVI_07720; -.
DR   OrthoDB; 9807643at2; -.
DR   Proteomes; UP000077013; 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   Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
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:UP000077013};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT   BINDING         83..88
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         133..140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         136
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         351
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         548
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         549
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         553
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         585..586
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         590
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         601..603
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         650
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   SITE            256
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT   SITE            421
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ   SEQUENCE   742 AA;  81916 MW;  91CB10385521D791 CRC64;
     MTKKAKIIYT KTDEAPALAT HSFLPIVEAF VTPSNIVVEA RDISLAARIL AQFSDLLSKE
     QQVNDALSEL GELAKQPDAN IIKLPNISAS MPQLTAAINE LQTKGYPLPD YPEDPANDEE
     KSIKAKYDKV KGSAVNPVLR EGNSDRRAPK AVKNFAKKHP HRMGAWDSDS KSHVATMGHG
     DFRNNEISVT LKEANTVKII HTDTTGNKTV LKDAIPVLKG EIIDATKMEK KALLSFLEDQ
     VKDAAAKNVL FSLHMKATMM KVSDPIIFGH AVKVYFKELF SKHKTTFDEL GVDVNNGFGD
     LTTKIEELPQ DKKEAILKDI EQIMDDQPDL AMVNSDKGIT NLHVPSDVII DASMPAMIRT
     SGQMWNADGK QQDTKAVIPD SSYASIYQAT INFCKEHGAF DPTTMGTVPN VGLMAQKAEE
     YGSHDKTFEI NSNGTVSVID DNGNTLIEHF VAEGDIWRMC QVKDLPIQDW IKLAVNRSRA
     TGSPAVFWLD EDRAHDAELI KKVNTYLPDH NTEGLEIKIL SPEKATLYTL ERVKEGKETI
     SVTGNVLRDY LTDLFPILEL GTSAKMLSIV PLMNGGGLFE TGAGGSAPKH VQQFVEEGHL
     RWDSLGEFLA LAVSLDHLGE TFNNPKATLM GEALDDATEK YLEHSKSPSR KVNELDNRGS
     HFYLALYWAQ ALANQDKDDV LKKRFTPIAE KLAKNETKIV SELNSAQGNS VDIGGYYEPN
     EALVSKEMRP SKTLNSILSE IK
//
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