ID A0A077EDT2_9FLAO Unreviewed; 548 AA.
AC A0A077EDT2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=3-Oxoadipate enol-lactonase, alpha/beta hydrolase fold family {ECO:0000313|EMBL:AIL44763.1};
GN ORFNames=BD94_0988 {ECO:0000313|EMBL:AIL44763.1};
OS Elizabethkingia anophelis NUHP1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Elizabethkingia.
OX NCBI_TaxID=1338011 {ECO:0000313|EMBL:AIL44763.1, ECO:0000313|Proteomes:UP000028933};
RN [1] {ECO:0000313|EMBL:AIL44763.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NUHP1 {ECO:0000313|EMBL:AIL44763.1};
RX PubMed=24012265; DOI=10.1016/S0140-6736(13)61858-9;
RA Teo J., Tan S.Y., Tay M., Ding Y., Kjelleberg S., Givskov M., Lin R.T.,
RA Yang L.;
RT "First case of E anophelis outbreak in an intensive-care unit.";
RL Lancet 382:855-856(2013).
RN [2] {ECO:0000313|EMBL:AIL44763.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NUHP1 {ECO:0000313|EMBL:AIL44763.1};
RX PubMed=26019164; DOI=10.1093/gbe/evv101;
RA Li Y., Liu Y., Chew S.C., Tay M., Salido M.M., Teo J., Lauro F.M.,
RA Givskov M., Yang L.;
RT "Complete Genome Sequence and Transcriptomic Analysis of the Novel Pathogen
RT Elizabethkingia anophelis in Response to Oxidative Stress.";
RL Genome Biol. Evol. 7:1676-1685(2015).
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DR EMBL; CP007547; AIL44763.1; -; Genomic_DNA.
DR RefSeq; WP_024565300.1; NZ_CP007547.1.
DR AlphaFoldDB; A0A077EDT2; -.
DR STRING; 1338011.BD94_0988; -.
DR KEGG; eao:BD94_0988; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_468316_0_0_10; -.
DR Proteomes; UP000028933; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR PANTHER; PTHR46331; VALACYCLOVIR HYDROLASE; 1.
DR PANTHER; PTHR46331:SF2; VALACYCLOVIR HYDROLASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF13715; CarbopepD_reg_2; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AIL44763.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..548
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001717610"
FT DOMAIN 341..450
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
SQ SEQUENCE 548 AA; 62061 MW; C9ACAB5BAE66242C CRC64;
MYKFGCITLL SLLSISAHAQ SVITGTVKNQ DNKTITYCSI GIKDSKTGTI TDGNGNYKLE
IPDEAKNKEI IFTAAGYSDK SIPANELKTN SNIVMDYKVT NIEAVVIGSK KLKEKTIGQK
SRPFLTFSKM FDQNVPTIEQ GNIFTVYQKT RLVAYNFYII PSSKFEQITM KLNIYSVKNN
EPDRPLLQEN VIYKTSTTGW QKIDLSEYKL NFNNLDKIAV TLQLVDHKAL PDIGFVFGIS
AKKSLSKNLL FRYQSQGNWE VSEGSFITNL DIRYDKAKGE KDITEEQDTD NDNDADTKAL
ISYYEHKKTA QKTVYGKNKE GKYIDLKDAK IYYEEYGKGQ PLILLHGNNG SISDFSKQIP
FFEKHYRVIA VDTRGQGRST DLTQDAYSYE KFASDLYQVI KSLNLEQVDI IGWSDGGNTA
LIFNYEHPEM VNRIVTIGAN MNPAGVKETL IELFKKQIIA NDPKTNPRLV KLMLNHPDIK
SNQLSVITNP VLVVAGSDDV IKDEHTRLIH KLIRNSELAI IPNATHYIPF EQPEKLNELM
LNFLKNKS
//
