ID D0LQ49_HALO1 Unreviewed; 456 AA.
AC D0LQ49;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen {ECO:0000313|EMBL:ACY17086.1};
GN OrderedLocusNames=Hoch_4595 {ECO:0000313|EMBL:ACY17086.1};
OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY17086.1, ECO:0000313|Proteomes:UP000001880};
RN [1] {ECO:0000313|EMBL:ACY17086.1, ECO:0000313|Proteomes:UP000001880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC {ECO:0000313|Proteomes:UP000001880};
RX PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL Stand. Genomic Sci. 2:96-106(2010).
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DR EMBL; CP001804; ACY17086.1; -; Genomic_DNA.
DR RefSeq; WP_012829684.1; NC_013440.1.
DR AlphaFoldDB; D0LQ49; -.
DR STRING; 502025.Hoch_4595; -.
DR KEGG; hoh:Hoch_4595; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_675960_0_0_7; -.
DR OrthoDB; 5516057at2; -.
DR Proteomes; UP000001880; 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; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001880};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..456
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003010332"
FT DOMAIN 269..447
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 22..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 456 AA; 48936 MW; 62C717C874CC245E CRC64;
MSFLWVAAAL LALSATSACN KDAKRDAGDT DEGVGAAAET AAGDTEVAAD SPAGEAARQW
YRAWFQGSPE VGEIPFFMQL PVAPLRGEVV VKQGDGLLRG EARWFGAEAS ANLPLLRTRL
YLRSDAKGQL SGHMTSASPV SDHAESLPLR AEPVDEVDNR KRFRDVAACG AAPEAANGQG
QGQDEPKAFA GEWLASFEER GEVGLSVVER EPGVWTGAAA FSNGTVVSLV GNAFGERLCL
SGFDGVNPTL MVLDLQAGGR RLSGRWAAGV SEETQSEFTA ERREQAIAHD TGGVRFTPNQ
TRLPLAKLGL AEFAGKPVII EFGASWCPPC LDAVPLFRSI YEAHHGNGLE IVTLLFELED
DDELLLRKAE AFTREYEIPW PVMPVRGEIA PYWKVVPHEP EVTEVNLPVT LFVNADGTIR
DAHMGFPPPN SGAPFDALRQ RYEAAAKELV GGGRGE
//
