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Database: UniProt
Entry: A0A0V0R127_PSEPJ
LinkDB: A0A0V0R127_PSEPJ
Original site: A0A0V0R127_PSEPJ 
ID   A0A0V0R127_PSEPJ        Unreviewed;       650 AA.
AC   A0A0V0R127;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Sugar-phosphate isomerase, RpiB/LacA/LacB family {ECO:0000313|EMBL:KRX08193.1};
GN   ORFNames=PPERSA_12348 {ECO:0000313|EMBL:KRX08193.1};
OS   Pseudocohnilembus persalinus (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC   Pseudocohnilembus.
OX   NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX08193.1, ECO:0000313|Proteomes:UP000054937};
RN   [1] {ECO:0000313|EMBL:KRX08193.1, ECO:0000313|Proteomes:UP000054937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=36N120E {ECO:0000313|EMBL:KRX08193.1};
RX   PubMed=26486372; DOI=10.1038/srep15470;
RA   Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA   Miao W.;
RT   "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT   persalinus provides insight into its virulence through horizontal gene
RT   transfer.";
RL   Sci. Rep. 5:15470-15470(2015).
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:KRX08193.1}.
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DR   EMBL; LDAU01000070; KRX08193.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0R127; -.
DR   EnsemblProtists; KRX08193; KRX08193; PPERSA_12348.
DR   InParanoid; A0A0V0R127; -.
DR   OrthoDB; 179137at2759; -.
DR   Proteomes; UP000054937; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR   Gene3D; 3.40.1400.10; Sugar-phosphate isomerase, RpiB/LacA/LacB; 1.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   InterPro; IPR003500; RpiB_LacA_LacB.
DR   InterPro; IPR036569; RpiB_LacA_LacB_sf.
DR   PANTHER; PTHR45847; FATTY ACID AMIDE HYDROLASE; 1.
DR   PANTHER; PTHR45847:SF6; FATTY ACID AMIDE HYDROLASE; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   Pfam; PF02502; LacAB_rpiB; 1.
DR   SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
DR   SUPFAM; SSF89623; Ribose/Galactose isomerase RpiB/AlsB; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Isomerase {ECO:0000313|EMBL:KRX08193.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054937};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        114..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          149..408
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
SQ   SEQUENCE   650 AA;  74621 MW;  A5AA86524142D09B CRC64;
     MWQTPNSKHD SNTQFSRTLF HSFDQNEDEE KFLNQPFIQD SFNSVHTEKL EHLNSPIKGE
     TQTLKQYKST EDLEKFKNLQ EIKNNNPYFR ERTISDERNF LIARAKKFHK NCKINLLSML
     IYFVILVISQ SFLFSYVRNT DLEDPKICET IQDKYYICDV NPEESFRVLK EIKEKYKNTE
     NKPPFYGVPF AVKNSINCKN FLNDFGCVNL LNYISQEDAV IVQILKEQGA IPICTTNISQ
     CYQGNTQNAI WGSPHNIFSD ERQAGGSSGG SCLLVANKLV PFALGSGSIK SPAIFNGVIG
     FCPSPCKISN IGVRSVLDGS FEQQTFHDIS MVIGPITKTV QDAIYFCQNT YQLSNCFDPY
     CSKQQFQILN SNPQFNNKKT INFGYVLKDS FCPLTQMQKN VIEETAPKEE ILEQLNSLKI
     LSKIPKFLKG KFLQYLIKII FGNRSSQFFR CFEPLSLQEY QQLLIKKDKL LKEFFQTWNK
     MEIDCLILPT TRFGVADLLD IDIFLDESYF TFSNAIHTCS GIVPLRLSTS KDITDVFDLA
     FNLAQKIREN SSNLGILITD NGILGSMVMN KQKGIRAGQC TNKYLAGMTR KHNNANVMVL
     GTDLVPLKQY QNFFKEFMEN QFDFSEETPQ HGKRVDKITK LEQNGVYKQI
//
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