ID A0A395SYZ0_9HYPO Unreviewed; 1116 AA.
AC A0A395SYZ0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=FLONG3_4574 {ECO:0000313|EMBL:RGP77339.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP77339.1, ECO:0000313|Proteomes:UP000266234};
RN [1] {ECO:0000313|EMBL:RGP77339.1, ECO:0000313|Proteomes:UP000266234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP77339.1,
RC ECO:0000313|Proteomes:UP000266234};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP77339.1}.
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; PXOG01000098; RGP77339.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395SYZ0; -.
DR STRING; 694270.A0A395SYZ0; -.
DR UniPathway; UPA00733; -.
DR Proteomes; UP000266234; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; 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; cd06503; ATP-synt_Fo_b; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 1.10.132.20; Ribosome-recycling factor; 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; IPR023584; Ribosome_recyc_fac_dom.
DR InterPro; IPR036191; RRF_sf.
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 Pfam; PF01765; RRF; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF55194; Ribosome recycling factor, RRF; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000266234};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 342..803
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 948..1112
FT /note="Ribosome recycling factor"
FT /evidence="ECO:0000259|Pfam:PF01765"
FT REGION 1097..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 580
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 1116 AA; 123811 MW; 24A757872D50573B CRC64;
MKLPFFSRSS QEHMDKPAKP NNYKVLFRKW PRKARKAVWW LMPLELMGVV PALVIFGISQ
PDLYRSDMWK IGWEHDPPLN SNPAIILYAY ANHRPLPKIA LVWTRTFTDF NVAISIISLF
FLLGKLTAFI MKCWYPIFAT FINASLVALY TVSTYGTIGP DYADSRYPAS AAWYYRVGCG
IARPYGKYKS CLIAKYSLVV CIYMLFIYLC NLGFSIYALL PNKINDVSDD DEEDEGSTTS
EPKERGVWEM HNMKTPDARA MPYTPRTQAF HTLDRQLPLR SQQHRGTMAL LQRLVAPSAR
GVLRQSPTIT LMITRKASNA SPPKLNDPSL LKQDVCYVNG EWVKAKSGKT FKVNDPSTGD
LIGTCPEFDS KDARLAIRAA ADAFPSFRNK TGRERSKLLR AWYDQMTANA EDIAKIITWE
NGKPMADAKG ETTYAANFLE WFSEEAPRLY GDVIPSSVPG NRVWTIKEPV GVCGLITPWN
FPAAMITRKI GPALAAGCTV VAKAPAETPF TSLALAELAH RAGIPKGVVN VVTSHENTPE
LGKLLTSDPT IRKVSFTGST NVGKLLMEQS ASTLKKLSLE LGGNAPFIVF DDADVDAAVA
GAIASKFRSS GQTCVCANRI YIQRGIYDEF VSKFTEKVKS FSVGNGFDQG VTHGPLIHDK
AIEKVEAHVK DAEKKGGKVT IGGKRLDDLG SNFYAPTVIR DMTPEMDMAS QETFGPVAGL
FPFETEEEVV KMANNTEVGL AGYFFSRDLE RVYRIAESLE VGMVGVNTGL ISDAAAPFGG
VKESGFGREG SLYGTSEYQI TKMITYGGMG ADASDFHNDS GLMNFDLDLD LRSTQNRFNH
NTLFEMAFSR ANAPLRTCLR QLVRSEGPAP LRSIATSPRT FSTSPFLLKK RKISAPANSP
NSANAKAAAG SMNKAEYDTA KVPMPDPEDP LDFTAVIAAY APIDAHFKTQ LAGMIHGGRF
NPTNLGSLPV AIKDEEGADA TFPLRELAQV VPRSGRAISL LVNDKEYIKP IMSAVQSSRE
FNQQPQRSED NELELLLKVE LERKDDVERR IKEAVQQWKD RIRNARSRHE KTLKDWKKNG
TVLPDIVKKA EKELQKVQDK KMKEIDQEEA QTIRQL
//
