ID A0A090LQ35_STRRB Unreviewed; 504 AA.
AC A0A090LQ35;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Succinate-semialdehyde dehydrogenase, mitochondrial {ECO:0000313|EMBL:CEF69656.1, ECO:0000313|WBParaSite:SRAE_2000430300.1};
GN ORFNames=SRAE_2000430300 {ECO:0000313|EMBL:CEF69656.1,
GN ECO:0000313|WBParaSite:SRAE_2000430300.1,
GN ECO:0000313|WormBase:SRAE_2000430300};
OS Strongyloides ratti (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=34506 {ECO:0000313|EMBL:CEF69656.1};
RN [1] {ECO:0000313|EMBL:CEF69656.1, ECO:0000313|Proteomes:UP000035682}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ED321 {ECO:0000313|Proteomes:UP000035682,
RC ECO:0000313|WBParaSite:SRAE_2000430300.1}, and ED321 Heterogonic
RC {ECO:0000313|EMBL:CEF69656.1};
RA Martin A.A.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|WBParaSite:SRAE_2000430300.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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; LN609529; CEF69656.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090LQ35; -.
DR STRING; 34506.A0A090LQ35; -.
DR EnsemblMetazoa; SRAE_2000430300.1; SRAE_2000430300.1; WBGene00264533.
DR WBParaSite; SRAE_2000430300.1; SRAE_2000430300.1; WBGene00264533.
DR WormBase; SRAE_2000430300; SRP08249; WBGene00264533; -.
DR eggNOG; KOG2451; Eukaryota.
DR OMA; VNGNWID; -.
DR OrthoDB; 216092at2759; -.
DR Proteomes; UP000035682; Chromosome X.
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; cd07103; ALDH_F5_SSADH_GabD; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
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; 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:UP000035682}.
FT DOMAIN 37..500
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 277
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 504 AA; 54813 MW; 3DAF31DC512DBDBA CRC64;
MNRQLLGNFK RFSINGKRFY ETILLPKGAR AFINGEWMKS ISGKTFPVLD PYTRETIYEA
SNCSISEAQI AVEASKQAFT SWSSQFTAKQ RGAILSEWGK LLMINQNALA ELMTREQGKP
LAEAKGEIAY AASYLDFYAA EALRVYGQVV PPNNLNRSHI HVKEPIGVVA VITPWNFPTA
MIARKAAAAL AVGCTMVVKP AEDTPLSALA FAELGEQSGI PNGVFNVIPA DLDNTKEISK
YLCSSKSISA ISFTGSTEVG KLLLEQSAST VKRVCLELGG NAPFIVFESA NIEKAVDGIM
ASKFRCSGQT CVSANRILIN EKIHDEFVEK LTRQIQKLKV GYGLDEGINF GPLINDKAIE
KVSRLVKDAK DKGATIQLGG QVAYEGTTLF SPTLIVGVTK DMSIAHEEIF GPVVAVQKFS
TEEEAIETAN STRSGLASYF YSQDISQIFR VQKALQFGMV GVNEGLISCS EAAFGGVKES
GMGREGGTQG IDEFTQWKYI CQTF
//