ID A7H799_ANADF Unreviewed; 664 AA.
AC A7H799;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=DSBA oxidoreductase {ECO:0000313|EMBL:ABS24595.1};
DE Flags: Precursor;
GN OrderedLocusNames=Anae109_0380 {ECO:0000313|EMBL:ABS24595.1};
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS24595.1, ECO:0000313|Proteomes:UP000006382};
RN [1] {ECO:0000313|EMBL:ABS24595.1, ECO:0000313|Proteomes:UP000006382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5 {ECO:0000313|EMBL:ABS24595.1,
RC ECO:0000313|Proteomes:UP000006382};
RX PubMed=25614562; DOI=10.1128/genomeA.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
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DR EMBL; CP000769; ABS24595.1; -; Genomic_DNA.
DR RefSeq; WP_011984701.1; NC_009675.1.
DR AlphaFoldDB; A7H799; -.
DR STRING; 404589.Anae109_0380; -.
DR KEGG; afw:Anae109_0380; -.
DR eggNOG; COG1651; Bacteria.
DR HOGENOM; CLU_016846_0_0_7; -.
DR OrthoDB; 9784686at2; -.
DR Proteomes; UP000006382; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR13887:SF14; CLPXP ADAPTER PROTEIN SPXH; 1.
DR PANTHER; PTHR13887; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR Pfam; PF01323; DSBA; 1.
DR Pfam; PF13462; Thioredoxin_4; 2.
DR SUPFAM; SSF52833; Thioredoxin-like; 3.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006382}.
FT DOMAIN 36..223
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 262..448
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 474..662
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 27..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 664 AA; 71837 MW; 05CF6B54BAE15125 CRC64;
MRHVSWIIAL VIGFSVGFFS RGAIDGGGRG ARPSGQAQQR PARPVEDPSA VYRVPVDDTP
LRGPADALVT IVESSDFECP FCKRVGPTLK QLEEAFPGKL RFSFRHNPLP FHARALPAAI
AAEEARAQGG DAKFWAMHDK LFELAPALDD ASIERAAQEI GIDAAKVKEA IASGKHKDRI
QRDQRVVQSV GAPATPSFFI NGRKLAGAQP FETFRALVAE ELKKAEALVQ GGTPASGVYA
KIMESASSRP VYLPTPTGQA APQDGAPKAP AAAPAAVYRK VPLRADDPAR GPASAKLTVV
LFSDFQCPFC ARVEPTLKQL EEAYPGQLRV VWKHQPLGFH QQAMPAALAA EAAREQGKFW
QLHDKLFENQ RALDDASLAR YAKEIGLDAR KLEQALQSKK HEPRIQEDMR LGASVGASGT
PTLFFNCRQL VGAQPFDRMK AVADEELKKA DALLGGARPD AGFYDRACDA NVAAAPAAPV
PAAAQAPAPG PIQKIDVRTD DPVRGNPKAP VTIVLFSDFQ CPFCARVGPT LDEVQRTYGD
KVRVVWKHQP LPFHQQALPA AEAAEAAREQ GRFWQMHDKL FASQRELSPD AYGRIAREIG
LDAKKFQASV QSGKARARIQ EDQQLASRVG AQGTPTMFVN GEKIVGAVPF AQIKAVIDRQ
LAAR
//
