ID A1WYD4_HALHL Unreviewed; 403 AA.
AC A1WYD4;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE SubName: Full=Beta-lactamase domain protein {ECO:0000313|EMBL:ABM62696.1};
GN OrderedLocusNames=Hhal_1932 {ECO:0000313|EMBL:ABM62696.1};
OS Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS halophila (strain DSM 244 / SL1)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Halorhodospira.
OX NCBI_TaxID=349124 {ECO:0000313|EMBL:ABM62696.1, ECO:0000313|Proteomes:UP000000647};
RN [1] {ECO:0000313|Proteomes:UP000000647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W.,
RA Richardson P.;
RT "Complete sequence of Halorhodospira halophila SL1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABM62696.1, ECO:0000313|Proteomes:UP000000647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647};
RX PubMed=23991253; DOI=10.4056/sigs.3677284;
RA Challacombe J.F., Majid S., Deole R., Brettin T.S., Bruce D., Delano S.F.,
RA Detter J.C., Gleasner C.D., Han C.S., Misra M., Reitenga K.G.,
RA Mikhailova N., Woyke T., Pitluck S., Nolan M., Land M.L., Saunders E.,
RA Tapia R., Lapidus A., Ivanova N., Hoff W.D.;
RT "Complete genome sequence of Halorhodospira halophila SL1.";
RL Stand. Genomic Sci. 8:206-214(2013).
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DR EMBL; CP000544; ABM62696.1; -; Genomic_DNA.
DR AlphaFoldDB; A1WYD4; -.
DR STRING; 349124.Hhal_1932; -.
DR KEGG; hha:Hhal_1932; -.
DR eggNOG; COG0491; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_030571_7_2_6; -.
DR OMA; AHFMIID; -.
DR OrthoDB; 9784009at2; -.
DR Proteomes; UP000000647; Chromosome.
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 Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
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:SF7; BETA-LACTAMASE DOMAIN PROTEIN; 1.
DR PANTHER; PTHR43084; PERSULFIDE DIOXYGENASE ETHE1; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000647}.
FT DOMAIN 20..131
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 403 AA; 44508 MW; DD2383E0883154E2 CRC64;
MLDTLKTAWT PAVAWEQLLG GGPLFILDVR NPDEFERWRV EGPHDTPTLN APYFELLDLD
DEDEDVNAAV LRGVRQQLTH QLPNDRTILT VCGEGHTSEH LADGLRELGY PALNLEGGME
AWGDFYYHRV VGNHERYTVY QVVRPARGDL SHVVISDGEA AVVDPNRHVE VYEELVHARG
ARITQVLDTH AHADHISGGP ELARRHRVPY YLHPYDAIHP MDMLPARIDF APLYAEQHVP
VGGITLRALH VPGHTLGMVA FLVDGQYLIA GDSIFLESIA RPDLGGAAEA WTPLFHESLQ
RLLALTEDTV VLPGHATDAG IADERGRFSA ELGALHRSNP GLRQVDAGLE SFRSYILGSL
PHFPEAYIEI KRVNIGLAHP DETEARRLEV GKNVCALSEA AAA
//