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Database: UniProt
Entry: V5FIN9_BYSSN
LinkDB: V5FIN9_BYSSN
Original site: V5FIN9_BYSSN 
ID   V5FIN9_BYSSN            Unreviewed;      1165 AA.
AC   V5FIN9;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|ARBA:ARBA00044146};
GN   ORFNames=PVAR5_0150 {ECO:0000313|EMBL:GAD91578.1};
OS   Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS   variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD91578.1, ECO:0000313|Proteomes:UP000018001};
RN   [1] {ECO:0000313|Proteomes:UP000018001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX   PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA   Oka T., Ekino K., Fukuda K., Nomura Y.;
RT   "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT   spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL   Genome Announc. 2:E0116213-E0116213(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAD91578.1}.
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DR   EMBL; BAUL01000002; GAD91578.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5FIN9; -.
DR   eggNOG; KOG2454; Eukaryota.
DR   HOGENOM; CLU_274743_0_0_1; -.
DR   InParanoid; V5FIN9; -.
DR   OrthoDB; 5743at2759; -.
DR   Proteomes; UP000018001; 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; 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; 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   Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018001}.
FT   DOMAIN          95..580
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   REGION          705..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          745..769
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..727
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        335
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   1165 AA;  128014 MW;  7E7983BCFD0E3107 CRC64;
     MDCIASHIPP WVLAAAEDLG LEPQWLSVGL VASCTLVAAY LGYAYLLCRR EAPVKFNVPL
     PPEVRPNWIA KKWDDVQGED KVLLEAQARG QWNEKKIMSY CPADGRVLGA SGPGIKPETA
     EGIDRAVQAA KRAQVEWAKT TFAERRRVLK TLLKYVLEHQ DEIVTACCLD SGKTKVDASF
     GEILVTTEKL KWTIDHGEKA LRTESRPTNF LMMYKKNTVR YEPLGVVSAC VSWNYPFHNF
     IGSVISGIFA GNGVVVKPSE QTAWCTGYFL DIVRGALISC GHPPDLVQSV VCLPNVADVL
     TSHPDISQLT FIGSRPVAHK VCESAAKALL PVTVELGGKD PSVILDDSTT IKQLPDIASI
     LMRGVFQSAG QNCIGVERVI ALPGVYDKLL DIVTPRIKAL RLGSIFLDSK PDPKDPSYKP
     ITPDVGAVIS LNGFDRLESL IEDAVKHGAR LICGGKRYNH PRHPHGHYFT PTLLADVTPS
     MRIAQTELFA PVFVLMRASS VPDAIAIANS TEYALGASVF GFNSRDVEAC VSGIKSGMVA
     VNDFGSYYAV QLPFGGVKGS GYGRFAGDEG LRGVSNVKAV CVDRFPRLMA TKIPPTVDYP
     IYKGDGDRKN GSGAWEMCKG VVETGYQLTL AGRASGIMKI LKNLDDGVAD GSDAVDDGHQ
     AAADGVEDRR NLLSGCWGAN DYPTISLASA VSTGMELTPI RVRGRRKRRA AANTKGLEEK
     ENAESKSVSL RRLKGGRPMM SFADKAASQS QTVARRHVPE KTSSGRRRRK LSRLECLPVE
     LIEKIFLYSL DVDLPRSSPA LAAALSRERM YRVFILLSFW NDVPVENDPA RPAIARILAP
     AEYERLDDER RKALQSDVLR CRWCTIQRIL AELPELMNFA IQKYWIGAGI TMDEINQRRF
     DHFLARNGGI RNFDGTGPNG NHYTLTVTPL LSIIVACVET QEINTYRILS VKGFPDGLLR
     GDDGFSDDDI AYLETLRTGH GFDAPGTDVS FSRDALQQGI HNALIEHNSR ALSALLKIDE
     YFTRHRLESE GTSSNTFYSI PPEHFHTAVT IAGDDPTLFQ LLLRTNAESL PADDSSITQW
     AMDLNSAFGS WLLDFMVQLP EHIDAARSDP RTAALFYMGR ANPDIELGRR YLDEVLGVTE
     LSSWLDETEF DVTSLWEAES SDSPS
//
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