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Database: UniProt
Entry: A0A178Z5Y7_9EURO
LinkDB: A0A178Z5Y7_9EURO
Original site: A0A178Z5Y7_9EURO 
ID   A0A178Z5Y7_9EURO        Unreviewed;       497 AA.
AC   A0A178Z5Y7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Succinate-semialdehyde dehydrogenase {ECO:0000256|RuleBase:RU365091};
DE            EC=1.2.1.16 {ECO:0000256|RuleBase:RU365091};
GN   ORFNames=AYL99_10879 {ECO:0000313|EMBL:OAP55179.1};
OS   Fonsecaea erecta.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1367422 {ECO:0000313|EMBL:OAP55179.1, ECO:0000313|Proteomes:UP000078343};
RN   [1] {ECO:0000313|EMBL:OAP55179.1, ECO:0000313|Proteomes:UP000078343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 125763 {ECO:0000313|EMBL:OAP55179.1,
RC   ECO:0000313|Proteomes:UP000078343};
RA   Weiss V.A., Vicente V.A., Raittz R.T., Moreno L.F., De Souza E.M.,
RA   Pedrosa F.O., Steffens M.B., Faoro H., Tadra-Sfeir M.Z., Najafzadeh M.J.,
RA   Felipe M.S., Teixeira M., Sun J., Xi L., Gomes R., De Azevedo C.M.,
RA   Salgado C.G., Da Silva M.B., Nascimento M.F., Queiroz-Telles F.,
RA   Attili D.S., Gorbushina A.;
RT   "Draft genome of Fonsecaea erecta CBS 125763.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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: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:OAP55179.1}.
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DR   EMBL; LVYI01000012; OAP55179.1; -; Genomic_DNA.
DR   RefSeq; XP_018688546.1; XM_018842385.1.
DR   AlphaFoldDB; A0A178Z5Y7; -.
DR   STRING; 1367422.A0A178Z5Y7; -.
DR   GeneID; 30015047; -.
DR   OrthoDB; 216092at2759; -.
DR   UniPathway; UPA00733; -.
DR   Proteomes; UP000078343; 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; 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   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.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078343}.
FT   DOMAIN          24..486
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        261
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   497 AA;  53067 MW;  5C753E7DCAF72EC7 CRC64;
     MHSAPKLKDP SLLISQAYIN GKFIDAASSE TFDVIDPGTG KKIGSCAELN KEDTNKAIAA
     ASDAFASFRK TLPRERATML RKWYDLMMEN ADDLATLITW ENGKPFNDAK GEVVYAANFF
     QWFSEEAPRI YGDTIGATVP GNRIMTWKQP VGVCGLITPW NFPAAMITRK IGPALAAGCT
     VVAKTPGETP FTANAIAELS RRAGVPPGVV NIVTAMKNTA EVGMVLTTDP RVKKVSFTGS
     TNVGKLLMKQ SSSTLKKLSF ELGGNAPFIV FDDVPDLDAA VAGAIACKFR SSGQTCVCAN
     RIYVQEGIYD AFAQKFTEKV KNFKVGYGFD DGVTHGPVIH DRAVAKVESH VQDATKKGGK
     VLCGGNKLTD LGSHFYAPTV IAGATNEMAI AHEETFGPVA GLFPFKTEKE VIALANDTEV
     GLAGYFYSRD IGRVYRVAEA LEVGMIGVNT GLISDGASPF GGVKQSGFGR EGSKYGVDEY
     VVIKSVTVGG ISNDLQE
//
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