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Database: UniProt
Entry: A0A080WE22_TRIRC
LinkDB: A0A080WE22_TRIRC
Original site: A0A080WE22_TRIRC 
ID   A0A080WE22_TRIRC        Unreviewed;       409 AA.
AC   A0A080WE22;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   03-MAY-2023, entry version 23.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   ORFNames=TERG_00818 {ECO:0000313|EMBL:KFL60391.1};
OS   Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559305 {ECO:0000313|EMBL:KFL60391.1, ECO:0000313|Proteomes:UP000008864};
RN   [1] {ECO:0000313|Proteomes:UP000008864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492}.
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DR   EMBL; GG700648; KFL60391.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A080WE22; -.
DR   VEuPathDB; FungiDB:TERG_00818; -.
DR   HOGENOM; CLU_005391_3_2_1; -.
DR   OMA; RHGKRWM; -.
DR   OrthoDB; 606537at2759; -.
DR   Proteomes; UP000008864; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43570:SF11; ALDEHYDE DEHYDROGENASE; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR036492};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008864};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..334
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ   SEQUENCE   409 AA;  44219 MW;  E7EB29BC915403DA CRC64;
     MKPTIRKDPL GCVLIIGAFN FPFVLTLGPL LGAIAAGNTV VVKPSEVSPH CAAVIQEIIE
     AALDPTCVSV VQGSVPETKA LLDERWDKIC FTGSARVGRI VAQAAAPKLT PVLLELGGRN
     PAFVTKRADL RLVARRLLWG KTFNAGQICI SQNYILVDRE VVDQLVVEFE RAIKEYYPNG
     AKASPDYSRI INEGAFQRIK QMVDNTKGKI LLGGSMDEKE KFIEPTVVLV DSTEDSLITE
     ESFGPIITLL PVSNLDEAIR IANDVDGTPL ALYPFGSKEE TAKVLSSVRS GGASVNDSYM
     HVSVANLPFG GVGESGTGCY HGRSSFDAFT HQRSITSTPG WVERILSIRY PPYIGKLGKY
     KAASLKSPNF NRAGERTYGL LEWITWFITF GKGPNRSGAA RATAAALGK
//
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