ID F2T8M3_AJEDA Unreviewed; 540 AA.
AC F2T8M3;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 2.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Succinate-semialdehyde dehydrogenase {ECO:0000256|RuleBase:RU365091};
DE EC=1.2.1.16 {ECO:0000256|RuleBase:RU365091};
GN ORFNames=BDDG_02527 {ECO:0000313|EMBL:EGE79586.2};
OS Ajellomyces dermatitidis (strain ATCC 18188 / CBS 674.68) (Blastomyces
OS dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=653446 {ECO:0000313|EMBL:EGE79586.2};
RN [1] {ECO:0000313|EMBL:EGE79586.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18188 {ECO:0000313|EMBL:EGE79586.2};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Genome Sequencing Center for Infectious Disease.;
RA Cuomo C., Klein B., Sullivan T., Heitman J., Young S., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A.M., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Blastomyces dermatitidis strain ATCC 18188.";
RL Submitted (MAR-2010) 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}.
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DR EMBL; GG749415; EGE79586.2; -; Genomic_DNA.
DR AlphaFoldDB; F2T8M3; -.
DR HOGENOM; CLU_005391_5_3_1; -.
DR UniPathway; UPA00733; -.
DR Proteomes; UP000007802; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..517
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 292
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 540 AA; 58026 MW; EE6978AA9F72ECA0 CRC64;
MNKLLRPLYN NPRSSYPFTI PVVSPVRRLA TMHTVPQLKD KSLFIEKCYV NGEWVGAQSG
QTFEVHDPST GKLIGTCPEF SVQDTQKAIH AAVAAFPSFR KTLARERARM LRRWYQLMMD
NADDIATLIT WENGKPIADA KGETNYAASF FEWFSEEAPR ICGDTIPSSV PGNRIMTMKE
PVGVCGFITP WNFPAAMITR KIGPALAAGC TVVAKSPGET PFTANAIAEL AHRAGIPKGV
VNIVTADKNT PEIGLCLTTH PEIRKVSFTG STNVGKLLMK QSSSTLKKLS FELGGNAPFI
VFDDCPDLDA AVAGAIASKF RSSGQTCVCA NRIYVQKGIY DEFAAKFAEK VKGFKLGHGF
SEGVTHGPVI HSRAVDKVSE HVLDATAQGA TVVVGGQKAP DLGSNFFHPT VLTGMTKDMK
LASEETFGPV AGLFAFETEK EVVDLANRAE VGLAGYFYSK DVARIFRVAE ALEVGMVGVN
TGIISDTAAP FGGIKQSGFG REGSKYGVDE FLTVKTVTFG SVGGPPSGII VLIILFALFD
//
