HOSM_SCHPO
ID HOSM_SCHPO Reviewed; 418 AA.
AC Q9Y823;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Homocitrate synthase, mitochondrial;
DE Short=HCS;
DE EC=2.3.3.14 {ECO:0000250|UniProtKB:O87198};
DE Flags: Precursor;
GN Name=lys4; ORFNames=SPBC1105.02c;
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).
CC -!- FUNCTION: Catalyzes the aldol-type condensation of 2-oxoglutarate with
CC acetyl-CoA to yield homocitrate. Carries out the first step of the
CC alpha-aminoadipate (AAA) lysine biosynthesis pathway.
CC {ECO:0000250|UniProtKB:O87198}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA +
CC H(+); Xref=Rhea:RHEA:12929, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58884; EC=2.3.3.14;
CC Evidence={ECO:0000250|UniProtKB:O87198};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12930;
CC Evidence={ECO:0000250|UniProtKB:O87198};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O87198};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O87198};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 1/5.
CC {ECO:0000250|UniProtKB:O87198}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. Homocitrate synthase LYS20/LYS21 subfamily. {ECO:0000305}.
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DR EMBL; CU329671; CAB50965.1; -; Genomic_DNA.
DR PIR; T39279; T39279.
DR RefSeq; NP_596458.1; NM_001022377.2.
DR PDB; 3IVS; X-ray; 2.24 A; A/B=1-418.
DR PDB; 3IVT; X-ray; 2.67 A; A/B=1-418.
DR PDB; 3IVU; X-ray; 2.72 A; A/B=1-418.
DR PDB; 3MI3; X-ray; 2.38 A; A/B=1-418.
DR PDBsum; 3IVS; -.
DR PDBsum; 3IVT; -.
DR PDBsum; 3IVU; -.
DR PDBsum; 3MI3; -.
DR AlphaFoldDB; Q9Y823; -.
DR SMR; Q9Y823; -.
DR BioGRID; 276365; 50.
DR STRING; 4896.SPBC1105.02c.1; -.
DR iPTMnet; Q9Y823; -.
DR MaxQB; Q9Y823; -.
DR PaxDb; Q9Y823; -.
DR PRIDE; Q9Y823; -.
DR EnsemblFungi; SPBC1105.02c.1; SPBC1105.02c.1:pep; SPBC1105.02c.
DR GeneID; 2539815; -.
DR KEGG; spo:SPBC1105.02c; -.
DR PomBase; SPBC1105.02c; lys4.
DR VEuPathDB; FungiDB:SPBC1105.02c; -.
DR eggNOG; KOG2367; Eukaryota.
DR HOGENOM; CLU_022158_2_2_1; -.
DR InParanoid; Q9Y823; -.
DR OMA; NTMRMLV; -.
DR PhylomeDB; Q9Y823; -.
DR BRENDA; 2.3.3.14; 5613.
DR UniPathway; UPA00033; UER00028.
DR EvolutionaryTrace; Q9Y823; -.
DR PRO; PR:Q9Y823; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; ISO:PomBase.
DR GO; GO:0004410; F:homocitrate synthase activity; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009085; P:lysine biosynthetic process; IDA:PomBase.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IMP:PomBase.
DR DisProt; DP02786; -.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_02222; Homocitr_synth_fung_arch; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011872; Homocitrate_synth_fun/arc.
DR InterPro; IPR000891; PYR_CT.
DR Pfam; PF00682; HMGL-like; 1.
DR TIGRFAMs; TIGR02146; LysS_fung_arch; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Lysine biosynthesis; Magnesium;
KW Manganese; Metal-binding; Mitochondrion; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..418
FT /note="Homocitrate synthase, mitochondrial"
FT /id="PRO_0000001049"
FT DOMAIN 35..288
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 321
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 43
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 103
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 163
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 197
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O87198"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:3IVT"
FT HELIX 25..29
FT /evidence="ECO:0007829|PDB:3IVS"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:3IVS"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:3IVS"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:3IVS"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:3IVS"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:3IVS"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:3IVS"
FT STRAND 97..106
FT /evidence="ECO:0007829|PDB:3IVS"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:3IVS"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:3IVS"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:3IVT"
FT HELIX 143..156
FT /evidence="ECO:0007829|PDB:3IVS"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:3IVS"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:3IVS"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:3IVS"
FT HELIX 174..187
FT /evidence="ECO:0007829|PDB:3IVS"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:3IVS"
FT HELIX 203..216
FT /evidence="ECO:0007829|PDB:3IVS"
FT STRAND 218..226
FT /evidence="ECO:0007829|PDB:3IVS"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:3IVS"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:3IVS"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:3IVS"
FT HELIX 263..273
FT /evidence="ECO:0007829|PDB:3IVS"
FT HELIX 275..281
FT /evidence="ECO:0007829|PDB:3IVS"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:3IVS"
FT HELIX 287..297
FT /evidence="ECO:0007829|PDB:3IVS"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:3IVS"
FT TURN 311..314
FT /evidence="ECO:0007829|PDB:3IVS"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:3IVS"
FT HELIX 320..324
FT /evidence="ECO:0007829|PDB:3IVS"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:3IVS"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:3IVS"
FT HELIX 337..340
FT /evidence="ECO:0007829|PDB:3IVS"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:3IVS"
FT HELIX 355..364
FT /evidence="ECO:0007829|PDB:3IVS"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:3IVS"
FT TURN 379..383
FT /evidence="ECO:0007829|PDB:3IVS"
FT HELIX 394..399
FT /evidence="ECO:0007829|PDB:3IVS"
SQ SEQUENCE 418 AA; 46293 MW; 55213523E4F46CDE CRC64;
MSVSEANGTE TIKPPMNGNP YGPNPSDFLS RVNNFSIIES TLREGEQFAN AFFDTEKKIQ
IAKALDNFGV DYIELTSPVA SEQSRQDCEA ICKLGLKCKI LTHIRCHMDD ARVAVETGVD
GVDVVIGTSQ YLRKYSHGKD MTYIIDSATE VINFVKSKGI EVRFSSEDSF RSDLVDLLSL
YKAVDKIGVN RVGIADTVGC ATPRQVYDLI RTLRGVVSCD IECHFHNDTG MAIANAYCAL
EAGATHIDTS ILGIGERNGI TPLGALLARM YVTDREYITH KYKLNQLREL ENLVADAVEV
QIPFNNYITG MCAFTHKAGI HAKAILANPS TYEILKPEDF GMSRYVHVGS RLTGWNAIKS
RAEQLNLHLT DAQAKELTVR IKKLADVRTL AMDDVDRVLR EYHADLSDAD RITKEASA
