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Database: UniProt
Entry: A0A0F4YNM7_TALEM
LinkDB: A0A0F4YNM7_TALEM
Original site: A0A0F4YNM7_TALEM 
ID   A0A0F4YNM7_TALEM        Unreviewed;       472 AA.
AC   A0A0F4YNM7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=homocitrate synthase {ECO:0000256|ARBA:ARBA00012974};
DE            EC=2.3.3.14 {ECO:0000256|ARBA:ARBA00012974};
GN   ORFNames=T310_6559 {ECO:0000313|EMBL:KKA19461.1};
OS   Rasamsonia emersonii CBS 393.64.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX   NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA19461.1, ECO:0000313|Proteomes:UP000053958};
RN   [1] {ECO:0000313|EMBL:KKA19461.1, ECO:0000313|Proteomes:UP000053958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA19461.1,
RC   ECO:0000313|Proteomes:UP000053958};
RA   Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA   Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000523};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12930;
CC         Evidence={ECO:0000256|ARBA:ARBA00000523};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 1/5.
CC       {ECO:0000256|ARBA:ARBA00004755}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. Homocitrate synthase LYS20/LYS21 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006361}.
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:KKA19461.1}.
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DR   EMBL; LASV01000346; KKA19461.1; -; Genomic_DNA.
DR   RefSeq; XP_013326073.1; XM_013470619.1.
DR   AlphaFoldDB; A0A0F4YNM7; -.
DR   STRING; 1408163.A0A0F4YNM7; -.
DR   GeneID; 25318860; -.
DR   OrthoDB; 2781767at2759; -.
DR   UniPathway; UPA00033; UER00028.
DR   Proteomes; UP000053958; Unassembled WGS sequence.
DR   GO; GO:0004410; F:homocitrate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR   CDD; cd07948; DRE_TIM_HCS; 1.
DR   Gene3D; 1.10.238.260; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_02222; Homocitr_synth_fung_arch; 1.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR048253; DRE_TIM_HCS_fun_bact.
DR   InterPro; IPR011872; Homocitrate_synth.
DR   InterPro; IPR000891; PYR_CT.
DR   NCBIfam; TIGR02146; LysS_fung_arch; 1.
DR   PANTHER; PTHR10277:SF48; HOMOCITRATE SYNTHASE, CYTOSOLIC ISOZYME-RELATED; 1.
DR   PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR   PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:KKA19461.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          65..324
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   472 AA;  51937 MW;  F32AB5D0D1777A8E CRC64;
     MSSGADNVPN GHTNGVNGNA NGDDIPPKEG FTAIRSRQNP FPSANRNPYG HNAGVTDFLS
     NVSRFKIIES TLREGEQFAN AFFDTQKKIE IAKALDDFGV DYIELTSPCA SEQSRRDCEA
     ICKLGLKAKS NRDAQILTHI RCHMDDARIA VETGVDGVDV VIGTSSYLRE HSHGKDMTYI
     TNTAIEVINF VKSKGIEVRF SSEDSFRSDL VDLLSIYSAV DQVGVNRVGI ADTVGCASPR
     QVYELVRVLR GVVKCDIECH FHNDTGCAIA NAYCALEGGA THIDTSVLGI GERNGITPLG
     GLMARMMVVA PDYVKNKYKL HKLKEIEDLV AEAVQVNIPF NNYITGFCAF THKAGIHAKA
     ILNNPSTYEI INPADFGMTR YVHFASRLTG WNAIKSRAQQ LNIEMTDEQY KECTAKIKAL
     ADIRPIAVDD ADSIIRAYHN NLKLGQNKPL LDLTEEEKAQ FEAKEKELAQ EA
//
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