ID   A0A1H4HIF3_9SPHI        Unreviewed;       585 AA.
AC   A0A1H4HIF3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
DE            EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194, ECO:0000256|PROSITE-ProRule:PRU00277};
GN   ORFNames=SAMN05443550_1215 {ECO:0000313|EMBL:SEB21647.1};
OS   Pedobacter hartonius.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=425514 {ECO:0000313|EMBL:SEB21647.1, ECO:0000313|Proteomes:UP000198850};
RN   [1] {ECO:0000313|EMBL:SEB21647.1, ECO:0000313|Proteomes:UP000198850}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19033 {ECO:0000313|EMBL:SEB21647.1,
RC   ECO:0000313|Proteomes:UP000198850};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC         Evidence={ECO:0000256|ARBA:ARBA00000971, ECO:0000256|PROSITE-
CC         ProRule:PRU00277};
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC       {ECO:0000256|ARBA:ARBA00006577}.
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DR   EMBL; FNRA01000021; SEB21647.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4HIF3; -.
DR   STRING; 425514.SAMN05443550_1215; -.
DR   OrthoDB; 1118217at2; -.
DR   Proteomes; UP000198850; Unassembled WGS sequence.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 3.10.50.40; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR000774; PPIase_FKBP_N.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR43811:SF19; 39 KDA FK506-BINDING NUCLEAR PROTEIN; 1.
DR   PANTHER; PTHR43811; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   Pfam; PF01346; FKBP_N; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW   ECO:0000313|EMBL:SEB21647.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198850};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW   ProRule:PRU00277}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..585
FT                   /note="peptidylprolyl isomerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011541712"
FT   DOMAIN          26..164
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          498..584
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
SQ   SEQUENCE   585 AA;  66551 MW;  3C70BEF098B884C4 CRC64;
     MKSKYILILA HLLIISSASA QSIKNLSIGD HLPDFVVKKI INYPKRSAKT SDFKNQLLIL
     DFWATSCSGC VFALPKMEKL QKQFANKIII LPVTYESKSL TSSFWRSNKY TKNLKIPSVV
     EDKLFSTYFK HKTIPHEVWV YNGKVIAITT PDYVNAEQIK KVLTGEPINW PVKYDFYRFD
     GSKPLFATDT NQIDLTSTSL KYAAISDYKE GINSEGLTGG SDILRDSVKK IVRAYFLNQP
     IYTSYLLNWM IVKPMNNLVK PGILVAPNQI VWEVADRSKY LFDPKLSYQQ EWIRKNGICF
     ESVNPDTGQT DQQVHQTIIS DLDRLLGLYV RWEKRKEKVW ILRKLDGGKN KLQKKGTDKI
     EELSTGGLVY FLNQQENNPY VFDETGIDKK LPLYISSWTN LPEIAAELND YGLKLEEQER
     EIDKLIFTEI DAGMLVDGQM QREFKAKRDA KINLTEIIPI ENQTFLENNK KQLGIKVTTS
     GLQYKILKEG TGPKPVPGCK IVVHYTGALI NGKIFDSSFE NGKASIFPIN DVIPGWMEAL
     QLMNKGSKWM LYIPASLAYG TGTAHGKLPP NSTLIFELEL LQILP
//