ID V2Y6M9_9FIRM Unreviewed; 402 AA.
AC V2Y6M9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR000108};
DE EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR000108};
GN ORFNames=GCWU0000282_000918 {ECO:0000313|EMBL:ESL03752.1};
OS Catonella morbi ATCC 51271.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Catonella.
OX NCBI_TaxID=592026 {ECO:0000313|EMBL:ESL03752.1, ECO:0000313|Proteomes:UP000018227};
RN [1] {ECO:0000313|EMBL:ESL03752.1, ECO:0000313|Proteomes:UP000018227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51271 {ECO:0000313|EMBL:ESL03752.1,
RC ECO:0000313|Proteomes:UP000018227};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUN-2013) 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:PIRNR000108};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRNR:PIRNR000108,
CC ECO:0000256|PIRSR:PIRSR000108-3};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRNR:PIRNR000108,
CC ECO:0000256|PIRSR:PIRSR000108-3};
CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC {ECO:0000256|PIRNR:PIRNR000108, ECO:0000256|PIRSR:PIRSR000108-3};
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 ECO:0000256|PIRNR:PIRNR000108}.
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:ESL03752.1}.
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DR EMBL; ACIL03000007; ESL03752.1; -; Genomic_DNA.
DR RefSeq; WP_023353801.1; NZ_KI535367.1.
DR AlphaFoldDB; V2Y6M9; -.
DR STRING; 592026.GCWU0000282_000918; -.
DR eggNOG; COG0538; Bacteria.
DR HOGENOM; CLU_023296_1_1_9; -.
DR OrthoDB; 9765655at2; -.
DR Proteomes; UP000018227; 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:0006102; P:isocitrate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.40.718.10; Isopropylmalate Dehydrogenase; 1.
DR InterPro; IPR004790; Isocitrate_DH_NADP.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR NCBIfam; TIGR00127; nadp_idh_euk; 1.
DR PANTHER; PTHR11822:SF21; ISOCITRATE DEHYDROGENASE [NADP], MITOCHONDRIAL; 1.
DR PANTHER; PTHR11822; NADP-SPECIFIC ISOCITRATE DEHYDROGENASE; 1.
DR Pfam; PF00180; Iso_dh; 1.
DR PIRSF; PIRSF000108; IDH_NADP; 1.
DR SMART; SM01329; Iso_dh; 1.
DR SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000108};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRNR:PIRNR000108};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000108}; NADP {ECO:0000256|PIRNR:PIRNR000108};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000108};
KW Reference proteome {ECO:0000313|Proteomes:UP000018227};
KW Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000108}.
FT DOMAIN 9..394
FT /note="Isopropylmalate dehydrogenase-like"
FT /evidence="ECO:0000259|SMART:SM01329"
FT BINDING 77
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT BINDING 94..100
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT BINDING 109
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT BINDING 132
FT /ligand="D-threo-isocitrate"
FT /ligand_id="ChEBI:CHEBI:15562"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-2"
FT BINDING 250
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-3"
FT BINDING 273
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-3"
FT SITE 139
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-1"
FT SITE 210
FT /note="Critical for catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000108-1"
SQ SEQUENCE 402 AA; 45700 MW; 6C1887A1CD929FCD CRC64;
MAKIEMKTPL VEMDGDEMTR VIWKMIKDEL IHPFINLKSE YYDLGLKYRN ETNDKVTAES
AQATLKYGVA VKCATITPNA ARVKEYELKE MWKSPNGTIR AMLDGTVFRT PILVKGIEPY
VRTWKEPITI ARHAYGDVYK NAEIKVNVPG KAELVFTAEN GTETRELIHE FKGAGVIQGI
HNLNSSIESF ARACFEYALE LKVDLWFSSK DTISKKYDHT FKDIFEEIYE KDYKEKFKNK
GITYFYTLID DAVARVVRSE GGFLWACKNY DGDVMSDMLA TAFGSLSMMT SVLVSPKGVW
EYEAAHGTVQ RHYYKYLKGE TTSTNSIATI FAWSGALRKR GELDGINELV NFADMLEKAV
IDTVESGTMT KDLADITTFK NVEVADTEEF IKAIRTKLEN LF
//
