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Database: UniProt
Entry: D7A9Z0_STAND
LinkDB: D7A9Z0_STAND
Original site: D7A9Z0_STAND 
ID   D7A9Z0_STAND            Unreviewed;       196 AA.
AC   D7A9Z0;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen {ECO:0000313|EMBL:ADH90777.1};
GN   OrderedLocusNames=Snov_3503 {ECO:0000313|EMBL:ADH90777.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM
OS   12100 / NBRC 12443 / NCIMB 10456).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Ancylobacter.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH90777.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|EMBL:ADH90777.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC
RC   12443 / NCIMB 10456 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A., Copeland A.,
RA   Berry K.W., Glavina Del Rio T., Hammon N., Dalin E., Tice H., Pitluck S.,
RA   Richardson P., Bruce D., Goodwin L.A., Han C., Tapia R., Detter J.C.,
RA   Chang Y.J., Jeffries C.D., Land M., Hauser L., Kyrpides N.C., Goker M.,
RA   Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic and
RT   methylotrophic alpha Proteobacterium Starkeya novella type strain (ATCC
RT   8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(2012).
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DR   EMBL; CP002026; ADH90777.1; -; Genomic_DNA.
DR   RefSeq; WP_013168278.1; NC_014217.1.
DR   AlphaFoldDB; D7A9Z0; -.
DR   STRING; 639283.Snov_3503; -.
DR   KEGG; sno:Snov_3503; -.
DR   eggNOG; COG0526; Bacteria.
DR   HOGENOM; CLU_042529_11_0_5; -.
DR   OrthoDB; 9799347at2; -.
DR   Proteomes; UP000006633; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
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; 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   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          41..181
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   196 AA;  20934 MW;  312A1D686EFD5E51 CRC64;
     MLAPEAPACR GTVTWYYSSV VAALALTTLG GGPLLARESP LPFGQGVPSL ALNSLNQGRQ
     DLAALQGKVV LVHFFATWCE PCREERAGLS RLAGRLPNRS FAVLAVDVGE VELRVRRFFD
     AHPVPFPVLL DEDRAALKAW KVVGLPSSFV LDPSHTLRLY AGGPVDWDDP EAVRLLESLA
     DPAGATAGGT LPPLDE
//
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