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Database: UniProt
Entry: H1Y748_9SPHI
LinkDB: H1Y748_9SPHI
Original site: H1Y748_9SPHI 
ID   H1Y748_9SPHI            Unreviewed;       376 AA.
AC   H1Y748;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen {ECO:0000313|EMBL:EHQ28667.1};
GN   ORFNames=Mucpa_4578 {ECO:0000313|EMBL:EHQ28667.1};
OS   Mucilaginibacter paludis DSM 18603.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=714943 {ECO:0000313|EMBL:EHQ28667.1, ECO:0000313|Proteomes:UP000002774};
RN   [1] {ECO:0000313|EMBL:EHQ28667.1, ECO:0000313|Proteomes:UP000002774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18603 {ECO:0000313|EMBL:EHQ28667.1,
RC   ECO:0000313|Proteomes:UP000002774};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Held B.,
RA   Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The permanent draft genome of Mucilaginibacter paludis DSM 18603.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CM001403; EHQ28667.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1Y748; -.
DR   STRING; 714943.Mucpa_4578; -.
DR   eggNOG; COG0526; Bacteria.
DR   HOGENOM; CLU_042529_1_0_10; -.
DR   OrthoDB; 6399635at2; -.
DR   Proteomes; UP000002774; Chromosome.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd02966; TlpA_like_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR025380; DUF4369.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   PANTHER; PTHR42852:SF6; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   Pfam; PF14289; DUF4369; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002774};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..376
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003558375"
FT   DOMAIN          238..376
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   376 AA;  42077 MW;  4569CD4F21DD78FD CRC64;
     MKMIRTLIYS LTVMLMMQTL KAQNKHVGYE IKGQLVSIPD AAVVYLTAGS SVDSAVVVNG
     KFTFTGTVAE PVLSTLKLKH TIPAPDTYYA IKRNTYRLFL TNTKMVFLAA DSLNGGVVKG
     NKLHNEYLSY QAGLSTIYDQ MRPLNMSYYA YERENNVPMM QKIRPRLDSL GAIEFSYVTN
     YVRANPKSPV ALLAVQQFAK PIANPPDFPA AFALLDNSLK QTAAGKLLEL RMADENAFKV
     GDSMPNFSQP DTLGNIVQLS EFKGKYVLID FWASWCGPCR NESPNVKRAF DKYNDKGFMV
     MMISLDVSKP NWLAAIKQDG TQNFIQLCDM KYHQNTAAQL LKIKSIPQNF LIDPSGKIIG
     RNLHGVELMN ALQRIL
//
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