ID Q0ZKK3_9STAP Unreviewed; 554 AA.
AC Q0ZKK3;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Rhodanese domain-containing protein {ECO:0000259|PROSITE:PS50206};
OS Staphylococcus sp. 693-2.
OG Plasmid pLEW6932 {ECO:0000313|EMBL:ABG49271.1}.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=373067 {ECO:0000313|EMBL:ABG49271.1};
RN [1] {ECO:0000313|EMBL:ABG49271.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=693-2 {ECO:0000313|EMBL:ABG49271.1};
RC PLASMID=pLEW6932 {ECO:0000313|EMBL:ABG49271.1};
RX PubMed=16820486; DOI=10.1128/AEM.00354-06;
RA Williams L.E., Detter C., Barry K., Lapidus A., Summers A.O.;
RT "Facile recovery of individual high-molecular-weight, low-copy-number
RT natural plasmids for genomic sequencing.";
RL Appl. Environ. Microbiol. 72:4899-4906(2006).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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DR EMBL; DQ390456; ABG49271.1; -; Genomic_DNA.
DR RefSeq; WP_011867754.1; NC_009130.1.
DR RefSeq; YP_001096305.1; NC_009130.1.
DR AlphaFoldDB; Q0ZKK3; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Plasmid {ECO:0000313|EMBL:ABG49271.1}.
FT DOMAIN 461..545
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 554 AA; 62034 MW; B268B2C779A05601 CRC64;
MKKIVIIGSV AAGTSVAAKA RRNSEDVEIT VFDKDSDISY SVCGIPYYIG GNVSDIDELT
PRNAKWFKER FNIDIYTEYE VNKINDSDQT ITVTNLVNDE KMIQKYDELV LATGSSSKEL
PQLNSEEYNN VFKVKNINDA KAIYNYINDH DVQNITIVGG GFIGLEMLEQ LSNYNTSIVQ
RNTFMPHLDY DMSFMIQEYI EDKANVYTYN EIDIIDYDEN HTINRVSLKT GELIDTDLII
IGIGVTPNTK LAKEIGINIG ESGAIQTNKY LETNIPHIYA IGDAAESYNL ITGNPIYRPL
GSTANKMGRI LGDRLTGGNL EHKGILGTGI VRVFDMTIAQ TGLTEKEAID LDIDIDVLHN
VKPNRPEYMQ GQEMVIKAIF DKNNSKLLGA QIIGYEGVDK RIDVLATAIT FGAKAEDLFH
LDLAYAPPFS TTKDPVIYTG MIGHNITRGR KIITPEEVVK QKNDLLILDV RSPKQFEVDH
VDGAINVPLK TLRSYAKTLD ENQTIVTYCN KGTTGNAAQN VLINLGFKQV YNLSGGNKNY
QRYKRFQVER EKKN
//
