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Database: UniProt
Entry: A0A094FRK5_9PEZI
LinkDB: A0A094FRK5_9PEZI
Original site: A0A094FRK5_9PEZI 
ID   A0A094FRK5_9PEZI        Unreviewed;      1556 AA.
AC   A0A094FRK5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 55.
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=V500_03736 {ECO:0000313|EMBL:KFY93361.1};
OS   Pseudogymnoascus sp. VKM F-4518 (FW-2643).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420913 {ECO:0000313|EMBL:KFY93361.1, ECO:0000313|Proteomes:UP000029284};
RN   [1] {ECO:0000313|EMBL:KFY93361.1, ECO:0000313|Proteomes:UP000029284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4518 (FW-2643) {ECO:0000313|Proteomes:UP000029284};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC       {ECO:0000256|ARBA:ARBA00005176}.
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:KFY93361.1}.
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DR   EMBL; JPKC01001171; KFY93361.1; -; Genomic_DNA.
DR   STRING; 1420913.A0A094FRK5; -.
DR   HOGENOM; CLU_003835_0_0_1; -.
DR   UniPathway; UPA00733; -.
DR   Proteomes; UP000029284; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07103; ALDH_F5_SSADH_GabD; 1.
DR   CDD; cd12148; fungal_TF_MHR; 1.
DR   CDD; cd00067; GAL4; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_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   InterPro; IPR007219; Transcription_factor_dom_fun.
DR   InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR   InterPro; IPR001138; Zn2Cys6_DnaBD.
DR   NCBIfam; TIGR01780; SSADH; 1.
DR   PANTHER; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43353:SF5; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   Pfam; PF04082; Fungal_trans; 1.
DR   Pfam; PF00172; Zn_clus; 1.
DR   SMART; SM00906; Fungal_trans; 1.
DR   SMART; SM00066; GAL4; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
DR   PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR   PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029284};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          336..366
FT                   /note="Zn(2)-C6 fungal-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50048"
FT   REGION          290..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..323
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1318
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   1556 AA;  170774 MW;  D8CCD3CBC2CE1280 CRC64;
     MLSPKKTIFA PHLGGIEVGY RLSATTPDLS KPTVVLFNPF TATADYYLPE FENKTLTDAL
     NLLAIEPLGH GQTRAKRTDT FTYWDSAIMG LQILEMLGIE HAYALGTSQG GWIAARMALL
     APERIKGIIL IGSSMDYESP RSRELGCWDG PAACSGLVAL NGDLTPAHDF EPGDAYYDFL
     MEIGFGKNVD KATRGFWAKT IRDNYNGDEG KKRVSMAAVN LASRDGLHER LPNIRCPILW
     LQGTDDVVFS FKNAEEEIKL FINSAKTRLW KGGERASLAP RSADLISGVD AKDLPVMSNT
     DQEQRSEPSR YSDAASPRRS TDSSAPTGKR RRVALACSNC RHRKSRCDGG RPKCSLCNEL
     GCDCLYEQAG TTSSLTVGRG YISRLEQRLE DIEEALKGLQ QPQNVSRSDT SYSIHDDAGL
     LPNNGASTGG ESSSRVPFRP VIGNTEISEV DTAEDSIDGM GAIKFTDEED CGYFGPSSNI
     AFVGHISLAM TRANAPSPVV PSPSNRARVA TGLLSVSRPH HVSQEVNASG LDRLHGGVNI
     YALPSEPRAW SLIRKYFLKT GQLLPFIHEQ SFCETYFQMK RDNCTMARRT WLGLLNIVFA
     MAATLSIDGD MSSEKRIEES DVYYQRANSL CDKESRRNIS VELVQYLLIS GQYLQGTQKS
     VQAWTVHGLA ITAAFQLGLH SPRANQDFSP LEREIRKRVW FGCILLDRTL SMTFGRPAII
     PETYVKLDLP NILMQIVGNT TQNEASPQMD AVFYTATIKL YSVMYHIIDS CYGQNLGFQD
     SSTNMEAVSL VLAGERQLEE WKQQLLPLLY LRVSEEPFGA QDLDKMDSNN QIVERFNVVL
     SLRFHNLRIL LHRPFLEKFL NDYSGNDSNT QSTENKILHQ VGINSVQTCV NSAKIIISIV
     RTVVSSTDWH RDLLGAWNYS LFYAFNASLV VFGALLVAPK DSSLNSHWGF VEQSRPYFSM
     AIEALRNLDR GNRVVERCVQ YLSQLSSALA GPTNPSDMAP NYCSLNMDPF TSQSGSACVL
     QQMQSLKQLP MDMELSEFMI NTDMDFLGGY IDVNRHYVDG QEIKDSTLFI QKGYVNGEWV
     NAQSGKTFGV YNPATTKIIG TCPEFSKADT EAAIRAAETA FTSFRNTTSR ERARLLQKWY
     HLMVENSEDL ANLITWESGK ALCDARTEVT YAASFLEWFS EEAPRTYGDV IPASIPGNRV
     FAFKEPIGVC GLITPWNFPA AMVTRKVGPA LAAGCTVVIK SPGETPFTVN ALIELARRAG
     IPKGVINIAT AASNTVEVGH TLTSSPIIRK ISFTGSTAVG KLMMRQCAET TLKKVSLELG
     GNAPFIVFND ADVDTAVAGA ISSKFRSSGQ TCVCPNRLIV QDDIYDIFAA KLAAKVREFK
     VGDSLETDGV THGPLIHDRA VAKVQSHVHD AEAKGGKVLV GGRKRPDLGP NFFEPTVITE
     MTEAMLLASD ETFGPVAGLF RFKTEADAVA LANKTDVGLA GYLFSKDIQR IWRVSEALQV
     GMIGVNTGLI SDPATPFGGV KSSGIGKEGS KYGIGEYMVT KVVTLGGMGI PLSSHL
//
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