LYS12_SCHPO
ID LYS12_SCHPO Reviewed; 362 AA.
AC O14104;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Homoisocitrate dehydrogenase;
DE Short=HICDH;
DE EC=1.1.1.87;
GN Name=lys12; ORFNames=SPAC31G5.04;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81 AND SER-91, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
RX PubMed=22105743; DOI=10.1002/prot.23231;
RA Bulfer S.L., Hendershot J.M., Trievel R.C.;
RT "Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces
RT pombe.";
RL Proteins 80:661-666(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-homoisocitrate + NAD(+) = 2-oxoadipate + CO2 + NADH;
CC Xref=Rhea:RHEA:11900, ChEBI:CHEBI:15404, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57499, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.87;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P40495};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P40495};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 4/5.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC dehydrogenases family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11688.1; -; Genomic_DNA.
DR PIR; T38621; T38621.
DR RefSeq; NP_594004.1; NM_001019430.2.
DR PDB; 3TY3; X-ray; 1.85 A; A/B=1-362.
DR PDB; 3TY4; X-ray; 1.55 A; A/B=1-362.
DR PDBsum; 3TY3; -.
DR PDBsum; 3TY4; -.
DR AlphaFoldDB; O14104; -.
DR SMR; O14104; -.
DR BioGRID; 279063; 22.
DR STRING; 4896.SPAC31G5.04.1; -.
DR iPTMnet; O14104; -.
DR MaxQB; O14104; -.
DR PaxDb; O14104; -.
DR PRIDE; O14104; -.
DR EnsemblFungi; SPAC31G5.04.1; SPAC31G5.04.1:pep; SPAC31G5.04.
DR GeneID; 2542609; -.
DR KEGG; spo:SPAC31G5.04; -.
DR PomBase; SPAC31G5.04; lys12.
DR VEuPathDB; FungiDB:SPAC31G5.04; -.
DR eggNOG; KOG0785; Eukaryota.
DR HOGENOM; CLU_031953_0_1_1; -.
DR InParanoid; O14104; -.
DR OMA; KLFRQPS; -.
DR PhylomeDB; O14104; -.
DR UniPathway; UPA00033; UER00030.
DR PRO; PR:O14104; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; ISS:PomBase.
DR GO; GO:0047046; F:homoisocitrate dehydrogenase activity; ISS:PomBase.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0009085; P:lysine biosynthetic process; IMP:PomBase.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR InterPro; IPR024084; IsoPropMal-DH-like_dom.
DR Pfam; PF00180; Iso_dh; 1.
DR SMART; SM01329; Iso_dh; 1.
DR PROSITE; PS00470; IDH_IMDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; Lysine biosynthesis;
KW Magnesium; Metal-binding; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..362
FT /note="Homoisocitrate dehydrogenase"
FT /id="PRO_0000310374"
FT BINDING 79..81
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:Q72IW9"
FT BINDING 81
FT /ligand="(2R,3S)-homoisocitrate"
FT /ligand_id="ChEBI:CHEBI:15404"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q72IW9"
FT BINDING 97
FT /ligand="(2R,3S)-homoisocitrate"
FT /ligand_id="ChEBI:CHEBI:15404"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q72IW9"
FT BINDING 107
FT /ligand="(2R,3S)-homoisocitrate"
FT /ligand_id="ChEBI:CHEBI:15404"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q72IW9"
FT BINDING 126
FT /ligand="(2R,3S)-homoisocitrate"
FT /ligand_id="ChEBI:CHEBI:15404"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q72IW9"
FT BINDING 133
FT /ligand="(2R,3S)-homoisocitrate"
FT /ligand_id="ChEBI:CHEBI:15404"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q72IW9"
FT BINDING 196
FT /ligand="(2R,3S)-homoisocitrate"
FT /ligand_id="ChEBI:CHEBI:15404"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q72IW9"
FT BINDING 198
FT /ligand="(2R,3S)-homoisocitrate"
FT /ligand_id="ChEBI:CHEBI:15404"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q72IW9"
FT BINDING 198
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:Q72IW9"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q72IW9"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q72IW9"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q72IW9"
FT BINDING 289..293
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:Q72IW9"
FT BINDING 301
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250|UniProtKB:Q72IW9"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT STRAND 6..15
FT /evidence="ECO:0007829|PDB:3TY4"
FT HELIX 18..30
FT /evidence="ECO:0007829|PDB:3TY4"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3TY4"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:3TY4"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:3TY4"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:3TY4"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:3TY4"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:3TY4"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:3TY4"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:3TY4"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:3TY4"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:3TY4"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:3TY4"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:3TY4"
FT HELIX 157..179
FT /evidence="ECO:0007829|PDB:3TY4"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:3TY4"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:3TY4"
FT HELIX 203..214
FT /evidence="ECO:0007829|PDB:3TY4"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3TY4"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:3TY4"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:3TY4"
FT HELIX 231..240
FT /evidence="ECO:0007829|PDB:3TY4"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:3TY4"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:3TY4"
FT HELIX 252..263
FT /evidence="ECO:0007829|PDB:3TY4"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:3TY4"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:3TY4"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:3TY4"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:3TY4"
FT TURN 292..296
FT /evidence="ECO:0007829|PDB:3TY4"
FT HELIX 303..315
FT /evidence="ECO:0007829|PDB:3TY4"
FT HELIX 319..335
FT /evidence="ECO:0007829|PDB:3TY4"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:3TY4"
FT HELIX 349..359
FT /evidence="ECO:0007829|PDB:3TY4"
SQ SEQUENCE 362 AA; 39256 MW; 85865AFD69BCE773 CRC64;
MSATRRIVLG LIPADGIGKE VVPAARRLME NLPAKHKLKF DFIDLDAGWG TFERTGKALP
ERTVERLKTE CNAALFGAVQ SPTHKVAGYS SPIVALRKKM GLYANVRPVK SLDGAKGKPV
DLVIVRENTE CLYVKEERMV QNTPGKRVAE AIRRISEEAS TKIGKMAFEI AKSRQKIRES
GTYSIHKKPL VTIIHKSNVM SVTDGLFRES CRHAQSLDPS YASINVDEQI VDSMVYRLFR
EPECFDVVVA PNLYGDILSD GAASLIGSLG LVPSANVGDN FVMSEPVHGS APDIAGRGIA
NPVATFRSVA LMLEFMGHQD AAADIYTAVD KVLTEGKVLT PDLGGKSGTN EITDAVLANI
HN
