ID Q1MQM2_LAWIP Unreviewed; 572 AA.
AC Q1MQM2;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Rhodanese-related sulfurtransferase {ECO:0000313|EMBL:CAJ54705.1};
GN Name=nadh {ECO:0000313|EMBL:CAJ54705.1};
GN OrderedLocusNames=LI0651 {ECO:0000313|EMBL:CAJ54705.1};
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253 {ECO:0000313|EMBL:CAJ54705.1, ECO:0000313|Proteomes:UP000002430};
RN [1] {ECO:0000313|EMBL:CAJ54705.1, ECO:0000313|Proteomes:UP000002430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00 {ECO:0000313|EMBL:CAJ54705.1,
RC ECO:0000313|Proteomes:UP000002430};
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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; AM180252; CAJ54705.1; -; Genomic_DNA.
DR RefSeq; WP_011526734.1; NC_008011.1.
DR AlphaFoldDB; Q1MQM2; -.
DR STRING; 363253.LI0651; -.
DR KEGG; lip:LI0651; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_003291_1_2_7; -.
DR OrthoDB; 9769238at2; -.
DR Proteomes; UP000002430; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00158; RHOD; 1.
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 PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000002430}.
FT DOMAIN 515..570
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 572 AA; 62597 MW; 99DFB59F81966EA7 CRC64;
MSKRVIIIGA IAAGPKAASR LRRLEPTTEI LMVDKNEYIS FGACGIPYYI SGEINSIDSL
RSTAYGVLRT PEYFQQKGIT TYNRTQAISI DRKQQIVLLK HLLTNKEYTV SYDKLVLTTG
SKPKLPTIKG QHLKHIVTIS NTSLDSAQHI QTLCASKKIK HAVIIGGGFI GLEMAVSLAG
KWKIKTSIIE VKPQVMPGYV SPDFADMLCH DLTKNNVEIF TSEQVLQFKG KNDSVNYLIT
DKRKIETDLV IFATGFLPET TLAQEAGLAL DPKTGAILVN PYMQTSDPNI YAGGDCVAVP
NPITGEHSWF TLGSLANRQG RIIGTNLAGG SDTFPGAVGN WCIKLFTLSA CGAGLTLEKA
KSLGFDAISA SIEQADRSQS YPEHSIISLE LIVDCSNRRV LGIQGICSAS DVVKARIDAI
TMLLQYGHPT IDDISNAEMS YAPPFSSAMD PINVVANVAD NILSGQLESV TSKTFTTMWN
DRKNNTIFFV DTRPTTASKE LKEKYPNEWH TIPFEEISSY LSELPKTQPI ALICNTGLRA
YETMSYLRGK GITNTIDVLG GMYAIKKRGE EL
//
