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
//