ID Q39YA0_GEOMG Unreviewed; 445 AA.
AC Q39YA0;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Rhodanese homology domain pair protein {ECO:0000313|EMBL:ABB30774.1};
GN OrderedLocusNames=Gmet_0531 {ECO:0000313|EMBL:ABB30774.1};
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799 {ECO:0000313|EMBL:ABB30774.1, ECO:0000313|Proteomes:UP000007073};
RN [1] {ECO:0000313|EMBL:ABB30774.1, ECO:0000313|Proteomes:UP000007073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC {ECO:0000313|Proteomes:UP000007073};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABB30774.1, ECO:0000313|Proteomes:UP000007073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15
RC {ECO:0000313|Proteomes:UP000007073};
RX PubMed=19473543; DOI=10.1186/1471-2180-9-109;
RA Aklujkar M., Krushkal J., DiBartolo G., Lapidus A., Land M.L., Lovley D.R.;
RT "The genome sequence of Geobacter metallireducens: features of metabolism,
RT physiology and regulation common and dissimilar to Geobacter
RT sulfurreducens.";
RL BMC Microbiol. 9:109-109(2009).
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DR EMBL; CP000148; ABB30774.1; -; Genomic_DNA.
DR RefSeq; WP_004512227.1; NC_007517.1.
DR AlphaFoldDB; Q39YA0; -.
DR STRING; 269799.Gmet_0531; -.
DR KEGG; gme:Gmet_0531; -.
DR eggNOG; COG2897; Bacteria.
DR HOGENOM; CLU_620750_0_0_7; -.
DR Proteomes; UP000007073; Chromosome.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:InterPro.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 2.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR InterPro; IPR045078; TST/MPST-like.
DR NCBIfam; NF040901; SeO3_TeO2_ExtH; 1.
DR PANTHER; PTHR11364:SF27; SULFURTRANSFERASE; 1.
DR PANTHER; PTHR11364; THIOSULFATE SULFERTANSFERASE; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 2.
DR PROSITE; PS00380; RHODANESE_1; 1.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007073};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 104..210
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 320..369
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 445 AA; 46810 MW; E390040F266F8F9E CRC64;
MAKQAWRKGR IILSGMLGVV ALAMLTLWGC GGGGGKSYDT PSLNGPAPVA TKTATPLVDA
VTLKGWLDAG LVNKAAGSER VVILEFSGSY VDTSVTPNVT KLRYNDGHIP GAIRVDLTAE
LMANRVEGPA EFAQMVASGA QMDALIKRCG IDENTTIVFT TSEAEMNSNT LWNITRPYTT
FRYWGFPKER LKVLDGGNKA WVAAAYPMTT VAPTITASTY NVTPLNTNRV KANLRASLSE
MIAAVNAGTG LIIDGRTDGV PGSTTDLVES SKYVVFEGRM TGGSGYSHVN LVDATTKKFK
DPAVVAADMT TKGLDLTKNT IYAMCRAGNI ASALFFYFDG ILYNDGSKNV VWYDGSWGQW
GLMSDNAAKG GKLPVGSAWA TDSLTLPITY DADLGRTVVD ITYRLDPTVS HATATANQIE
DADKAYLSPV TSGGGGAGGG GGGGC
//
