ID   K1XVN6_MARBU            Unreviewed;       638 AA.
AC   K1XVN6;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00044146};
GN   ORFNames=MBM_05218 {ECO:0000313|EMBL:EKD16749.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD16749.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD16749.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD16749.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00024149};
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; JH921438; EKD16749.1; -; Genomic_DNA.
DR   RefSeq; XP_007293107.1; XM_007293045.1.
DR   AlphaFoldDB; K1XVN6; -.
DR   STRING; 1072389.K1XVN6; -.
DR   GeneID; 18761153; -.
DR   KEGG; mbe:MBM_05218; -.
DR   eggNOG; KOG2450; Eukaryota.
DR   HOGENOM; CLU_005391_0_1_1; -.
DR   InParanoid; K1XVN6; -.
DR   OMA; HGIGYYP; -.
DR   OrthoDB; 216092at2759; -.
DR   Proteomes; UP000006753; 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   CDD; cd07091; ALDH_F1-2_Ald2-like; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
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.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        88..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          168..628
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        405
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   638 AA;  69449 MW;  C4BA16F66E887731 CRC64;
     MLGCAVQVTA SRRGDYVMTD GLREDYRDLV DGLLICRSRI AGKSSEMRGS RLGNGNAPPS
     LAFACGSCLS INSIKSPTLS IPRASQSLFS LLFLFLFLFL FLFLFLFLFH IPNIPIPIAS
     GKTTTTHLLI SRYLLHFPPL EKMTVIELST PSTGKYKQPT ALFINNEWVK GVDGKTFETI
     NPSTEEVICS VHEATEKDVD IAVAAARKAF DGPWRKVTPE NRGRCLVNLA NLLEKNADLL
     AAVESLDNGK SLSMAKDDVT AVVGCLRYYG GWSDKIEGKV IETNSDTFSY TKQEPIGVCG
     QIIPWNFPLL MWSWKIGPAV AAGNTVVLKT AEQTPLSALV AASFIKEAGF PPGVINIISG
     FGRVAGAAIS AHMDVDKVAF TGSTVVGRQV MKAAAGSNLK KVTLELGGKS PNIVFNDADI
     ENAISWVNFG IFFNHGQCCC AGSRVYVQSG IYDKFIQRFK ERAAANKVGD PFHPDTFQGP
     QISQLQYDRI MGYIEEGKKS GATIVTGGER HGDKGYFIQP TIFADVTEDM KIMQEEIFGP
     VCSISKFETE EEILKTGNNT SYGLAAAVHT TNLNTAIRVS NGLRAGTVWV NQYNMLHWQL
     PFGGYKESGI GRELGEAALA NYTQTKTVSI RLGDALFG
//