ID C9SU15_VERA1 Unreviewed; 482 AA.
AC C9SU15;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Aldehyde dehydrogenase {ECO:0000313|EMBL:EEY22326.1};
GN ORFNames=VDBG_08436 {ECO:0000313|EMBL:EEY22326.1};
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN [1] {ECO:0000313|Proteomes:UP000008698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC {ECO:0000313|Proteomes:UP000008698};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
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; DS985225; EEY22326.1; -; Genomic_DNA.
DR RefSeq; XP_003001391.1; XM_003001345.1.
DR AlphaFoldDB; C9SU15; -.
DR STRING; 526221.C9SU15; -.
DR GeneID; 9529444; -.
DR KEGG; val:VDBG_08436; -.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_0_1; -.
DR OMA; IVPLMKW; -.
DR OrthoDB; 216092at2759; -.
DR Proteomes; UP000008698; Unassembled WGS sequence.
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; cd07106; ALDH_AldA-AAD23400; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR044086; LUC3-like.
DR PANTHER; PTHR11699:SF263; ALDEHYDE DEHYDROGENASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000008698}.
FT DOMAIN 24..473
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 246
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 482 AA; 52196 MW; 16AF66F7E82317B8 CRC64;
MADSQFTFSN LINGVLRPGA SVTQGINPSD RKPLWDVPLA SRQDLEDAVA AAKDAFPAWK
KTTWAERSRI VSAIRDVLLE NSEQMATLLT KEVGKPIEFA RIEVDHSSNF LQFNAGLPEP
EEKITLDDET LRLSIRQQPV GVVVAICPWN FPLVLAVAKI AAALITGNCI ILKPSPFTPY
SVLKFAELTN HLLPKGVLQV LHGDANLGPW MCSHPGVDKI TFTGSTATGK KIMVNAAETL
KTITLELGGN SASIVCGDVN PKIVAPQVAM GAFFNSGQYC LASKRIYVHE SIYDEFLAEI
VSTVKGWKVG PTSDLEEGIM LGPVQNEMQY GIVHSFFSEA VDNGFKFALG GPIPKAEDVK
NFIVPPAIID NPPDESLVVK GEAFGPILPI LKWSTEDEVL KRVNDTQTGL GGTVWSSDLV
RARAIAERVE SGTIWINSFE KPLPHAHLNG HKESGVGGEW GAEGLGSYLK PQVIHSYKAS
PV
//