ID K1MB37_9FLAO Unreviewed; 469 AA.
AC K1MB37;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Rhodanese domain-containing protein {ECO:0000259|PROSITE:PS50206};
GN ORFNames=HMPREF9699_00182 {ECO:0000313|EMBL:EKB59613.1};
OS Bergeyella zoohelcum ATCC 43767.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Bergeyella.
OX NCBI_TaxID=883096 {ECO:0000313|EMBL:EKB59613.1, ECO:0000313|Proteomes:UP000006085};
RN [1] {ECO:0000313|EMBL:EKB59613.1, ECO:0000313|Proteomes:UP000006085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43767 {ECO:0000313|EMBL:EKB59613.1,
RC ECO:0000313|Proteomes:UP000006085};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bergeyella zoohelcum ATCC 43767.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKB59613.1}.
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DR EMBL; AGYA01000005; EKB59613.1; -; Genomic_DNA.
DR RefSeq; WP_002661595.1; NZ_JH932293.1.
DR AlphaFoldDB; K1MB37; -.
DR STRING; 883096.HMPREF9699_00182; -.
DR PATRIC; fig|883096.3.peg.180; -.
DR eggNOG; COG0491; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_030571_7_1_10; -.
DR OrthoDB; 9784009at2; -.
DR Proteomes; UP000006085; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050313; F:sulfur dioxygenase activity; IEA:InterPro.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR CDD; cd07724; POD-like_MBL-fold; 1.
DR CDD; cd00158; RHOD; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 2.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR044528; POD-like_MBL-fold.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR43084; PERSULFIDE DIOXYGENASE ETHE1; 1.
DR PANTHER; PTHR43084:SF1; PERSULFIDE DIOXYGENASE ETHE1, MITOCHONDRIAL; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF00581; Rhodanese; 2.
DR SMART; SM00849; Lactamase_B; 1.
DR SMART; SM00450; RHOD; 2.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 2.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006085}.
FT DOMAIN 268..359
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 372..456
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 469 AA; 51405 MW; 6FD9087AFEC53E0F CRC64;
MKIEQIYTGC LAQGAYYIVS GKEAAIIDPL REVQPYLDRL DEDGVVLKYI FETHFHADFV
SGHLDLSKKT GAPIVYGPTA QPSFEAIIAE DNQIFQIGDI KIKVLHTPGH TMESATFLLI
DENGKETAIF SGDTLFLGDV GRPDLAQKAA NLTQEELAGL LYDSLYTKIL PLADDITVYP
AHGAGSACGK NMQKETVDTL GNQKKTNYAL NQPNKEAFIE AVLDGLTAPP QYFGMNVAMN
KGGYESFEEV MDKGMKALEP NEFEAIAEQT GALILDTRSA AEFHKGFIPN AINIGLKGDF
APWVGAMIVD VKHPILLVTD EGTEEEAITR LSRVGFDNVL GYLKGGFAAW KATGKETDEV
KRISPETFVN EFSPEAKIID VRKPTEYAAE HIENAYSRPL NDIAQWAGGI SNDEHFYLHC
AGGYRSMIAA SILNKRGIRN FTEIEGGFGG IKKTEKIPTT DFVCQSKTL
//
