ID A0A161VPY0_9PEZI Unreviewed; 501 AA.
AC A0A161VPY0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Succinate-semialdehyde dehydrogenase {ECO:0000256|RuleBase:RU365091};
DE EC=1.2.1.16 {ECO:0000256|RuleBase:RU365091};
DE Flags: Fragment;
GN ORFNames=CI238_04295 {ECO:0000313|EMBL:KZL79194.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL79194.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL79194.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL79194.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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:KZL79194.1}.
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DR EMBL; LFIW01002127; KZL79194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A161VPY0; -.
DR STRING; 1573173.A0A161VPY0; -.
DR UniPathway; UPA00733; -.
DR Proteomes; UP000076584; 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:UP000076584}.
FT DOMAIN 34..496
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 272
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZL79194.1"
SQ SEQUENCE 501 AA; 53525 MW; FA4CAC09227FB762 CRC64;
LLIFTMASGA NQLTPVELRD ASLLKTSCYV NGKWVGANSG KVFSVENPST LVEVAGCPEF
DEVDTEASIL AAYDAFKSYR KTPARVRARL LRKWYDLMME NAEDLATIIT LENGKPMADA
RTEVAYAASF FEWFSEEAPR IYGDTIQASN PSCRLVTLKE PIGVCGLIAP WNFPAAMITR
KVGPALAAGC TVVVKAPAEA PLTALALAEL AHRAGIPAGV VNIITALDNT VSVGKVLTTH
PVIKKVSFTG STGVGKLLMN QCSSTLKKLS FELGGNAPFI VFEDADLDAA LKGLIASKFR
ISGQTCVCAN RILVHSKVYE KFSHMVVDAI KSFVVGDGFG EKTTHGPLIH SRAVSKVDEH
VKDAVSKGAR VLLGGKPRAE LGPNFFDLTV LADMKPGMKI CSEETFGPVA AFFAFETEEE
AVKLANDADV GLAGYFFSKD VSRCWRVAEA LEVGMVGVNI GAISDPAAPF GGVKQSGFGR
EGSKYGIDEF LVTKMVMTGI E
//
