GenomeNet

Database: UniProt
Entry: A0A090LQ35_STRRB
LinkDB: A0A090LQ35_STRRB
Original site: A0A090LQ35_STRRB 
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
//
DBGET integrated database retrieval system