ID A0A0D9VCS5_9ORYZ Unreviewed; 1177 AA.
AC A0A0D9VCS5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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};
DE AltName: Full=Trimethylguanosine synthase {ECO:0000256|ARBA:ARBA00018517};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR02G04860.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR02G04860.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR02G04860.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR02G04860.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(2),N(7)-dimethyl 5'-triphosphoguanosine)-
CC ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end
CC (N(2),N(2),N(7)-trimethyl 5'-triphosphoguanosine)-(ribonucleoside) in
CC mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67624,
CC Rhea:RHEA-COMP:17171, Rhea:RHEA-COMP:17315, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:167623,
CC ChEBI:CHEBI:172880; Evidence={ECO:0000256|ARBA:ARBA00024488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67625;
CC Evidence={ECO:0000256|ARBA:ARBA00024488};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(2),N(7)-dimethyl 5'-
CC triphosphoguanosine)-ribonucleoside in mRNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67620, Rhea:RHEA-COMP:17167, Rhea:RHEA-
CC COMP:17315, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:156461, ChEBI:CHEBI:172880;
CC Evidence={ECO:0000256|ARBA:ARBA00024618};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67621;
CC Evidence={ECO:0000256|ARBA:ARBA00024618};
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC Trimethylguanosine synthase family. {ECO:0000256|ARBA:ARBA00025783}.
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 AlphaFoldDB; A0A0D9VCS5; -.
DR STRING; 77586.A0A0D9VCS5; -.
DR EnsemblPlants; LPERR02G04860.1; LPERR02G04860.1; LPERR02G04860.
DR Gramene; LPERR02G04860.1; LPERR02G04860.1; LPERR02G04860.
DR eggNOG; KOG2451; Eukaryota.
DR eggNOG; KOG2730; Eukaryota.
DR HOGENOM; CLU_273462_0_0_1; -.
DR Proteomes; UP000032180; Chromosome 2.
DR GO; GO:0008168; F:methyltransferase activity; 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 GO; GO:0009452; P:7-methylguanosine RNA capping; IEA:InterPro.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd07103; ALDH_F5_SSADH_GabD; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR019012; RNA_cap_Gua-N2-MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_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; PF09445; Methyltransf_15; 1.
DR Pfam; PF00397; WW; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000032180}.
FT DOMAIN 338..366
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 42..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 948
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 1177 AA; 128401 MW; 933BF8BDEF0E959A CRC64;
MPAEAEEIPP AIRRLGRHFR LTEVHLWDDW YCSAGAAEVG GHTSWRSSVD TTGSGDHLTD
KIQNKAPKQT DEGHPSVEDL ELANLMGSLG LPVSFSTSKE VSVDNNTSFY SKVSIAEALL
PLQKKNAPNK VKKNRRKVYY EAENITGDDL RTFTGTKEIE SAVQLMACIE QTNPCSSSRS
TVGCNEVCQG DSEKMGKDNG YANEQEESGC GYLCSAKVLS SSEAESKCEL NQLTSQSHAN
TNNPLKADSP VQDNQTGEVV LQLNKEMLEQ NSIDNECRIS SGRLSTIEDQ LSGGTPSTSH
DNSDVNHETC LSSEEPSPVD NNPTQMSDSS FYFEYGDWRV LWDPFYSRYY FYNILTQEST
WYPPRGLEDF ASHSSTHIPD GLDELGSQSK SIPAQEHDQA GGDKHLDGQG QDCYSILSNL
SDITDEERIN QCMVSFTDEA CHTDSIQNDS SMSEISEMHL EVARTKKKKR VRRSKSYHSC
QGLAENVSND IAKYWTQRYS LFSLFDSGIK MDGEGWFSVT PELIAKHHAS RIGAGVVIDC
FTGVGGNAIH FAMKCKHVIA IDIDQQKIDC AQHNATVYGV NDYIDFITAD FIDTAPHLKG
ETAFMSPPWG GPDYAKVDAY DINTMLKPCD GYSLFKLGTS IASRVVMFLP RNIDQNQLAD
MCLSVDPPWA VEVEKNFLNG KLKAITAYFE QQDDSDLQLA SDSVNMTVDA GAAVERVRAA
GLLKTQGLIG GKWVDAYDGK MLEVQNPATG EILANVSCMG SKETSDAIAS AHSTFYSWSK
LTASERSKVL RKWHDLIISH KEELALLMTL EQGKPMKEAL GEVTYGASFI EYFAEEAKRI
YGDIIPPTLS DRRLLVLKQV GPALACGCTV VVKPSEFTPL TALAAADLAL QAGIPPGALN
VVMGNAPEIG DSLLQSTQVR KITFTGSTAV GKKLMAGSAN TVKKVSLELG GNAPCIVFDD
ADIDVAIKGS LAAKFRNSGQ TCVCANRILV QEGIYEKFAS VFVKAVQSLQ VGNGLEESTS
QGPLINEAAV QKVEKFINDA TSKGANIMLG GKRHSLGMTF YEPTVVGNVS NDMLLFRDEV
FGPVAPLIPF KTEEDAIHMA NDTNAGLAAY IFTKSIPRSW RVSEALEYGL VGVNEGLIST
EVAPFGGVKQ SGLGREGSKY GVDEYLELKY ICMGNLN
//
