ID S3DCF5_GLAL2 Unreviewed; 1290 AA.
AC S3DCF5;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Succinate-semialdehyde dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00019842};
DE EC=1.2.1.24 {ECO:0000256|ARBA:ARBA00013051};
DE AltName: Full=NAD(+)-dependent succinic semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00030806};
GN ORFNames=GLAREA_10453 {ECO:0000313|EMBL:EPE34759.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE34759.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE34759.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
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DR EMBL; KE145356; EPE34759.1; -; Genomic_DNA.
DR RefSeq; XP_008078694.1; XM_008080503.1.
DR STRING; 1116229.S3DCF5; -.
DR GeneID; 19469500; -.
DR KEGG; glz:GLAREA_10453; -.
DR eggNOG; KOG1399; Eukaryota.
DR eggNOG; KOG1577; Eukaryota.
DR eggNOG; KOG2451; Eukaryota.
DR HOGENOM; CLU_262305_0_0_1; -.
DR OrthoDB; 49786at2759; -.
DR Proteomes; UP000016922; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
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 Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR018170; Aldo/ket_reductase_CS.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43353:SF5; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR Pfam; PF00743; FMO-like; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000016922}.
FT DOMAIN 596..1044
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 1052..1255
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
SQ SEQUENCE 1290 AA; 142215 MW; 64724C07F33105FF CRC64;
MVSSRSPNAI IIGAGPSGIA LAYKLKHTLG FEDFTLYEKL DGPGGTWRTN TYPGCGCDIP
THLYSFSFNL NSNWSKVLAD QPEILQYMED TVDKFSLRSH ILSSVECLGA EWNKETSLWH
VKFRDLLTKI EYTRTATILV SCVGGISFPR DVKFKGKENF KGSMFHTAEW DHSVNYKGKR
MAVIGNGCSA AQVVPNIAGK VSFVKQYARS AQWYHDRPNK RYSEFEKFAF RVVPLWMRLL
RLSIFLDADA QSTTYLPTPA GIKARAKAEA ESKEYIHGKT PKKYHDFVVP TFALGCKRRI
FDPDYLDCLN RPNVDLVAEG ISEITEDGII SSTGTKDVFD IIVLATGFQV SQFLTPMKVI
GKQGISLNQQ WRECRGAQAY LGTYVHNFPN MAIIFGPNTF PANNSALFSC EVQVDFAIKS
LFIPILDRRV SVIEVKQSAE DRETAKIHDG LRNTVFSGAC SNWYIGDFGR NAASWAGTAA
SFWRKTYFPQ WNAFYMEGGE KLWWLNTMRR WVRNLSWQSR LSVLVVAAFY GYHTSLLSRF
SVDTPSVELP MVPETGWNLV SVGGGELDIS GRSWTCTCST EGSEFEVASG GFSNFTEPVG
GSKISQVASF NEHEFNTAIE SAKIAQQHYY TSTTAAQRVA LFRNWYELVI KNKKDLAIIL
CLENGKTLLE AEAEVVYAAD FIAWFAAEAP RSYGDSIPSS IPNTTVMTLK QPIGVCGIIT
PWNFPAAMIT GKIAPALAAG CAVVIKPPKE TPHTCLALVK LAIEAGLPPK AIQVCTTSNR
QAATMLATHP SISKLSFTGS TGVGKMLAKL AAGTLKKCSL ELEGNAPFIV FDDANLDHAV
EAAMICKFRC TGQTCVCANR LLVHKAVVKE FTSKLVQKVS ELSIGSGINS KTTQGPLVNR
AAVDKVREHV EDAIAKGGKV EIGGYARNTS GLFFLPTVLT GATRQMKIAT EETFGPLAAI
FEFTTEDEAI RLANDTEFGL AGYFFNRDIG RILRVSRELQ CGMVGVNTGK ISAAKSPFGG
IKESGYGREG SKYGMAEYEI LKTITIGNTD VHIDAAYCYE NEVEVGQGLT EAFQAGIKRR
DVFVTTKLWS TFHSRVEEAL DESLKNLGLD YVNLYLMHWP VAMNPNAHGK ASRYGKVKAI
GVANFSVKYL EELLGHVSVV PAVNQTENHP FLPQYDNVDF CKQKDIHITA YSPLGSAGSS
LLTDEGIKKI ADEYRVSAST ILISFHISRG LSVLAKSVNP LRINSNKEVV EINCMDLKAL
KTLAAKRGFV TRYVYPAFGI DFGFPDKKNH
//
