GenomeNet

Database: UniProt
Entry: F2C7G7_STRSA
LinkDB: F2C7G7_STRSA
Original site: F2C7G7_STRSA 
ID   F2C7G7_STRSA            Unreviewed;       403 AA.
AC   F2C7G7;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|ARBA:ARBA00019562, ECO:0000256|RuleBase:RU004446};
DE            EC=1.1.1.42 {ECO:0000256|ARBA:ARBA00013013, ECO:0000256|RuleBase:RU004446};
GN   Name=icd {ECO:0000313|EMBL:EGF14454.1};
GN   ORFNames=HMPREF9386_1108 {ECO:0000313|EMBL:EGF14454.1};
OS   Streptococcus sanguinis SK330.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=888813 {ECO:0000313|EMBL:EGF14454.1, ECO:0000313|Proteomes:UP000005955};
RN   [1] {ECO:0000313|EMBL:EGF14454.1, ECO:0000313|Proteomes:UP000005955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK330 {ECO:0000313|EMBL:EGF14454.1,
RC   ECO:0000313|Proteomes:UP000005955};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (FEB-2011) 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|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:EGF14454.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AFBD01000004; EGF14454.1; -; Genomic_DNA.
DR   RefSeq; WP_002915661.1; NZ_GL878548.1.
DR   AlphaFoldDB; F2C7G7; -.
DR   PATRIC; fig|888813.3.peg.1090; -.
DR   HOGENOM; CLU_031953_7_1_9; -.
DR   Proteomes; UP000005955; Unassembled WGS sequence.
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:EGF14454.1};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU004446}.
FT   DOMAIN          24..395
FT                   /note="Isopropylmalate dehydrogenase-like"
FT                   /evidence="ECO:0000259|SMART:SM01329"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-1"
FT   BINDING         288
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-3"
FT   BINDING         335
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-2"
FT   SITE            154
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT   SITE            224
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-4"
FT   MOD_RES         94
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT   MOD_RES         107
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
FT   MOD_RES         136
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604439-5"
SQ   SEQUENCE   403 AA;  44197 MW;  1BD7B81A02A6F1B2 CRC64;
     MEGDKMADKI LFENGRLLVP DAPIIPYIQG DGIGIDIWRN AQLVFDKAVE KAYGGQRKVV
     WKEVLAGKKA ADLTGDWLPD ETLTTIKSHL VAIKGPLETP VGEGIRSLNV ALRQELDLYA
     CLRPVRYFKG VPSPLKHPEK TDITIFRENT EDIYAGIEWE SGTAEVQKVI DFLQKDMQVD
     KIRFPESSAI GIKPISKQGS ERLIRAAIDY ALAKGLTRVT LVHKGNIQKF TEGGFRKWGY
     ELAQREYADE LASGKLIIQD VIADNFLQQI LLYPEKFDVV ALTNLNGDYA SDALAAQVGG
     IGIAPGANIN YETGHAIFEA THGTAPDIAG QNKANPCSLL LSGAMLFDYI GWPEVSHLLT
     KAIEKALFEQ KVTGDFASHL EGVAALTTGQ FAEELLANIE KCS
//
DBGET integrated database retrieval system