ID A3LYG4_PICST Unreviewed; 616 AA.
AC A3LYG4;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Meiotic Sister-Chromatid recombination aldehyde dehydrogenase {ECO:0000313|EMBL:ABN67974.2};
DE EC=1.2.1.3 {ECO:0000313|EMBL:ABN67974.2};
DE EC=1.2.1.39 {ECO:0000313|EMBL:ABN67974.2};
DE EC=1.2.1.9 {ECO:0000313|EMBL:ABN67974.2};
GN Name=MSC7 {ECO:0000313|EMBL:ABN67974.2};
GN ORFNames=PICST_90594 {ECO:0000313|EMBL:ABN67974.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN67974.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN67974.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986}.
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DR EMBL; CP000500; ABN67974.2; -; Genomic_DNA.
DR RefSeq; XP_001386003.2; XM_001385966.1.
DR AlphaFoldDB; A3LYG4; -.
DR STRING; 322104.A3LYG4; -.
DR GeneID; 4840166; -.
DR KEGG; pic:PICST_90594; -.
DR eggNOG; KOG2454; Eukaryota.
DR HOGENOM; CLU_005391_1_0_1; -.
DR InParanoid; A3LYG4; -.
DR OMA; ILMRGTF; -.
DR OrthoDB; 5743at2759; -.
DR Proteomes; UP000002258; Chromosome 6.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008886; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008957; F:phenylacetaldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR CDD; cd07098; ALDH_F15-22; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR PANTHER; PTHR11699:SF211; ALDEHYDE DEHYDROGENASE FAMILY 16 MEMBER A1; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:ABN67974.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 13..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..555
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 616 AA; 68804 MW; 44A9940D8F875540 CRC64;
MILLDFKFHE WQWQYQISTT FFVFGIVPFV FWVYARYITA SPNKYNKLEE PVKLSVPIPA
EAKPHWKGKR LYPPNLTIRA ANEPTKIQSY CPATGQYLGT FTATTRDEMN QQIANAKVAQ
KEWKASSFSL RRQVLKTLSR FILDNQEDIA RIACRDSGKT KLDASMGEIM VTLEKLKWII
AHGERVLRPS QRPGPSNLLI GMMKNGEVRY EPLGVVAALV SWNYPFHNLM GPIIAALFTG
NAIIVKCSEQ VIWSSTWYID LVRLVLKSLE IDPNLVQLCC CYAEDADHFT SHPGLSHITF
IGSKPVAHKV VESASKELTP VVVELGGKDS LIVLDDVKDI ESLSSVILRG TFQSAGQNCI
GVERVICLPK SYEKLVEIFT ERIKEFRLGS DIDQLDEIDM GAMISDNRFK QLEALVEDAV
SKGARLIHGG KPYQHPNYPQ GHYFEPTLIV DVDPSMRIFQ EEVFGPVLTM IKANDVDDAV
NLANGTEYGL GNSVFGSNFR QINEIANRLD SGNVAINDFA TFYVAQLPFG GIKKSGYGKF
GGEEGLLGLC VAKSVVMDKP IMRLFGVATS IPPPIDYPIK DDKRAWKFVS SLNTAGYDTR
VWNIIKAFKK LAKGGA
//
