ID B8GPA5_THISH Unreviewed; 460 AA.
AC B8GPA5;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=2-alkenal reductase {ECO:0000313|EMBL:ACL74025.1};
DE EC=1.3.1.74 {ECO:0000313|EMBL:ACL74025.1};
DE Flags: Precursor;
GN OrderedLocusNames=Tgr7_2953 {ECO:0000313|EMBL:ACL74025.1};
OS Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396588 {ECO:0000313|EMBL:ACL74025.1, ECO:0000313|Proteomes:UP000002383};
RN [1] {ECO:0000313|EMBL:ACL74025.1, ECO:0000313|Proteomes:UP000002383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-EbGR7 {ECO:0000313|EMBL:ACL74025.1,
RC ECO:0000313|Proteomes:UP000002383};
RX PubMed=21475584;
RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL Stand. Genomic Sci. 4:23-35(2011).
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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DR EMBL; CP001339; ACL74025.1; -; Genomic_DNA.
DR AlphaFoldDB; B8GPA5; -.
DR STRING; 396588.Tgr7_2953; -.
DR KEGG; tgr:Tgr7_2953; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_1_6; -.
DR Proteomes; UP000002383; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 2.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011782; Pept_S1C_Do.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR NCBIfam; TIGR02037; degP_htrA_DO; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Oxidoreductase {ECO:0000313|EMBL:ACL74025.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002383};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..460
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039528764"
FT DOMAIN 259..350
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 361..452
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 111
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 215
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 460 AA; 49107 MW; F60E4170F3552CCF CRC64;
MHPVHSKLRN TLTVFLCLLL LAMAPMASAT LPVEVDGEPL PSLAPMLDRT IPAVVNIATR
GRVVERNPLM EDPFFRRFFD LPQQPRERQT QGLGSGVILD AEQGYIITNF HVIQRADEIV
VTLHDGRRLD AEVVGTDPAT DLAVLRVQGD NLTAVKVADS DALRVGDFVV AIGNPFGLGQ
TVTSGIVSAL GRSGLGIESY EDFIQTDASI NPGNSGGALV NLRGELVGIN TAILSGGGGN
IGIGFAIPVN MALQVKDHLV AHGEVRRGRL GVTVQDLTPE LAQAFGISQT QGAVIAQVEP
GSAAERAGLK EGDVVLRVNE RRVRNATELR NAIGLLRVGS EVQLDVVRDN RRRTLTAVVA
EIRAATTEGA QFNRRLEGAS FSEITEASPL HGRVQGVLVT GVQSGSPAAR AGIREGDVIL
SVNRQPVSNL EEMRRAAGSN GQRLLLNIRR DEGAFFLILQ
//
