ID A0A1V6QJ64_9EURO Unreviewed; 493 AA.
AC A0A1V6QJ64;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Succinate-semialdehyde dehydrogenase {ECO:0000256|RuleBase:RU365091};
DE EC=1.2.1.16 {ECO:0000256|RuleBase:RU365091};
GN ORFNames=PENSOL_c065G06495 {ECO:0000313|EMBL:OQD89250.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD89250.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + succinate semialdehyde = 2 H(+) + NADH +
CC succinate; Xref=Rhea:RHEA:13217, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57706, ChEBI:CHEBI:57945; EC=1.2.1.16;
CC Evidence={ECO:0000256|RuleBase:RU365091};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) + succinate semialdehyde = 2 H(+) + NADPH +
CC succinate; Xref=Rhea:RHEA:13213, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57706,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.16;
CC Evidence={ECO:0000256|RuleBase:RU365091};
CC -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC {ECO:0000256|ARBA:ARBA00005176, ECO:0000256|RuleBase:RU365091}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU365091}.
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:OQD89250.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MDYO01000065; OQD89250.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6QJ64; -.
DR STRING; 60172.A0A1V6QJ64; -.
DR OrthoDB; 216092at2759; -.
DR UniPathway; UPA00733; -.
DR Proteomes; UP000191612; Unassembled WGS sequence.
DR GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0036243; F:succinate-semialdehyde dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07103; ALDH_F5_SSADH_GabD; 1.
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; IPR010102; Succ_semiAld_DH.
DR NCBIfam; TIGR01780; SSADH; 1.
DR PANTHER; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43353:SF5; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU365091};
KW Reference proteome {ECO:0000313|Proteomes:UP000191612}.
FT DOMAIN 24..487
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 493 AA; 53161 MW; 72616FCA69D6D1F5 CRC64;
MSHTVPQLKD KSLFIGKCHI NGEWVGAQSG KTFEITDPAT DKVIGTCPEF SAKDTERAIK
AASDAFPVFQ KTLVRERSRL LRRWNDLILQ NLDDLATLIT WENGKPFAEA QGEVKYAAAF
IEWFSEEAPR LYADTIPTSV PGNRVLTVKE PVGVCGLITP WNFPAAMITR KIGPALAAGC
TVVAKSPGET PFTANALAEL ALRAGIPKGV VNIVTALENT SEVGHTLTTH PDIKKVSFTG
STRVGKLLME QASSSVKRVS WELGGNAPFI VFDDVEDIDI AVAGALVSKF RGTGQTCVCA
NRIYIHRSHY KAFAKRLVER IKNFNVGPGF AEGVTHGPLI HRAAAQKVAD HVADAKSKGA
RVLLGGSPIN ELGPTFFQPT VLADMTHDMR IADEETFGPI AALFPFDTEE EVVQLANRCE
VGLAAYIFSD NIRRVFRVAD VLEVGMVGVN TGSVSDVAAP FGGVKESGFG REGSKYGIEE
FVNVKSITLG GIF
//
