ID B1FEZ3_9BURK Unreviewed; 401 AA.
AC B1FEZ3;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE SubName: Full=2-alkenal reductase {ECO:0000313|EMBL:EDT03871.1};
DE EC=1.3.1.74 {ECO:0000313|EMBL:EDT03871.1};
GN ORFNames=BamIOP4010DRAFT_2603 {ECO:0000313|EMBL:EDT03871.1};
OS Burkholderia ambifaria IOP40-10.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=396596 {ECO:0000313|EMBL:EDT03871.1, ECO:0000313|Proteomes:UP000005463};
RN [1] {ECO:0000313|EMBL:EDT03871.1, ECO:0000313|Proteomes:UP000005463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IOP40-10 {ECO:0000313|EMBL:EDT03871.1,
RC ECO:0000313|Proteomes:UP000005463};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA Tiedje J., Richardson P.;
RT "Sequencing of the draft genome and assembly of Burkholderia ambifaria
RT IOP40-10.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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:EDT03871.1}.
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DR EMBL; ABLC01000055; EDT03871.1; -; Genomic_DNA.
DR RefSeq; WP_006751792.1; NZ_ABLC01000055.1.
DR AlphaFoldDB; B1FEZ3; -.
DR MEROPS; S01.477; -.
DR GeneID; 69545506; -.
DR PATRIC; fig|396596.7.peg.5123; -.
DR Proteomes; UP000005463; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
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; 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 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:EDT03871.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 282..350
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 382..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 164
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 238
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 401 AA; 42144 MW; CB9D76AE27DCF034 CRC64;
MLRRFWLFFA QAVTVLLALM FIVVTLKPQW LQRQGQLGKQ LATPIVALRE VAPGIGGAPA
TTSYAEAAQK AMPAVVNVFS SKDGSLPPDP RAKDPLFRYF FGDRNARKQQ DEPAANLGSG
VIVSPEGYIL TNQHVVDGAD QIEVALADGR TATAKVIGSD PETDLAVLKI NMTNLPTITL
GRSDQSRVGD VVLAIGNPFG VGQTVTMGII SALGRNHLGI NTFENFIQTD APINPGNSGG
ALVDVNGNLL GINTAIYSRS GGSLGIGFAI PVSTARTVLE SIITTGSVTR GWIGVEPQDV
TPEIAESFGL QQKTGAIVAG VLQGGPADKA GIKPGDILVS VNGDEITDTT KLLNTVAQIK
PGTSTKVHVV RKGKEFDVNV VIGKRPPPPK QALDEQDSDS E
//