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Database: UniProt
Entry: C5FEJ2_ARTOC
LinkDB: C5FEJ2_ARTOC
Original site: C5FEJ2_ARTOC 
ID   C5FEJ2_ARTOC            Unreviewed;       549 AA.
AC   C5FEJ2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=methylmalonate-semialdehyde dehydrogenase (CoA acylating) {ECO:0000256|ARBA:ARBA00013048};
DE            EC=1.2.1.27 {ECO:0000256|ARBA:ARBA00013048};
GN   ORFNames=MCYG_01114 {ECO:0000313|EMBL:EEQ28226.1};
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ28226.1, ECO:0000313|Proteomes:UP000002035};
RN   [1] {ECO:0000313|Proteomes:UP000002035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
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).
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DR   EMBL; DS995701; EEQ28226.1; -; Genomic_DNA.
DR   RefSeq; XP_002851010.1; XM_002850964.1.
DR   AlphaFoldDB; C5FEJ2; -.
DR   STRING; 554155.C5FEJ2; -.
DR   GeneID; 9228471; -.
DR   VEuPathDB; FungiDB:MCYG_01114; -.
DR   eggNOG; KOG2449; Eukaryota.
DR   HOGENOM; CLU_005391_1_10_1; -.
DR   OMA; GGAKNHI; -.
DR   OrthoDB; 275238at2759; -.
DR   Proteomes; UP000002035; Unassembled WGS sequence.
DR   GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity; IEA:UniProtKB-EC.
DR   CDD; cd07085; ALDH_F6_MMSDH; 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   InterPro; IPR010061; MeMal-semiAld_DH.
DR   NCBIfam; TIGR01722; MMSDH; 1.
DR   PANTHER; PTHR43866; MALONATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43866:SF3; METHYLMALONATE-SEMIALDEHYDE DEHYDROGENASE [ACYLATING], MITOCHONDRIAL; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002035}.
FT   DOMAIN          63..527
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   REGION          23..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   549 AA;  58776 MW;  F642E02823E74086 CRC64;
     MASSRNTSAT AIRRLHAMAQ QLKPAAAATS TTSAASTATS FPQSHERIAS PIDTANFIDN
     EFTASRAETW IDLFDPATNN LVTRVPQSTE EEMKAAVASA QAAFPAWKAT SIMARQQIMF
     KFVNLIRANW DRLAASITLE QGKTFADAKG DVLRGLQVAE TACGITTQMT GEVLEVAKDM
     ETRSYREPLG VVSAICPFNF PAMIPLWCIP IATMTGNTLV MKPSERDPGA AMILAELARE
     AGFPKGVINI IHGSAKTVDF ILDAPEIKAI SFVGSNRAGE YIFTRGSANG KRVQANLGAK
     NHCAVLPDAN KNHALNAIAG AAFGAAGQRC MALSTLVMVG ETKEWLPEIA ERARALKVDG
     GFEEGADLGP VISPESKKRI EDIIATAEKE GATILLDGRG YKPEKYPNGN WVGPTIITGV
     KPHMTCYKEE IFGPVLVCLE VDTLDEAIDL INANEYGNGA AVFTRSGPTA TKFQRQIEAG
     QLGINVPIPV PLPMFSFTGN KKSIAGGGAN TFYGKPGLQF YTQQKTVTSL WRSEDAISNK
     ASVVMPTQS
//
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