ID A5UXN6_ROSS1 Unreviewed; 413 AA.
AC A5UXN6;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=2-alkenal reductase {ECO:0000313|EMBL:ABQ91389.1};
DE EC=1.3.1.74 {ECO:0000313|EMBL:ABQ91389.1};
GN OrderedLocusNames=RoseRS_3025 {ECO:0000313|EMBL:ABQ91389.1};
OS Roseiflexus sp. (strain RS-1).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Roseiflexus.
OX NCBI_TaxID=357808 {ECO:0000313|EMBL:ABQ91389.1, ECO:0000313|Proteomes:UP000006554};
RN [1] {ECO:0000313|Proteomes:UP000006554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS-1 {ECO:0000313|Proteomes:UP000006554};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Roseiflexus sp. RS-1.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP000686; ABQ91389.1; -; Genomic_DNA.
DR RefSeq; WP_011957733.1; NC_009523.1.
DR AlphaFoldDB; A5UXN6; -.
DR STRING; 357808.RoseRS_3025; -.
DR KEGG; rrs:RoseRS_3025; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_0_0_0; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000006554; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IEA:UniProtKB-EC.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:ABQ91389.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 302..398
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 47..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..67
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 41499 MW; ACBCD5D7B2388BA5 CRC64;
MERGTKFALI FGMIATLLIG ALIGALAGGG VAWYVTQQQI ERIAAQPTSP APVPVSAPAP
TVAPGNTPAP APTIAPAPTI APVAPASASP VVEVVQKVSP AVVTVVNTLA SGAQASPLLG
DLPFPLPDQP GGLVRRGSGS GVIISADGYI LTNNHVIEGH RSLSVIFYDG SRRDAKLIGA
DPLMDLAVVK VDGPVPGVAV LGDSDALQPG ETVIAIGSPL GDFRNTVTVG VVSALNRSLG
GNAPEGLIQT DAAINSGNSG GPLINLRGEV IGINTLVVRG GGLGSAPAEG LGFAVPSSIA
KRVSEQLIAN GKVVYPFLGV RFGTIDAMLA LDNNLPVNAG ALIAAVEPGG PAARAGLRSG
DIVTKVNGKP IGPGQSLRAL LLEYKPGDVV TLEVLRDSEQ LSLDVTLGTR PEA
//
