ID A0A154BM03_ANASB Unreviewed; 561 AA.
AC A0A154BM03;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:KYZ74945.1};
GN ORFNames=AXX12_15305 {ECO:0000313|EMBL:KYZ74945.1};
OS Anaerosporomusa subterranea.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Anaerosporomusa.
OX NCBI_TaxID=1794912 {ECO:0000313|EMBL:KYZ74945.1, ECO:0000313|Proteomes:UP000076268};
RN [1] {ECO:0000313|EMBL:KYZ74945.1, ECO:0000313|Proteomes:UP000076268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU4 {ECO:0000313|EMBL:KYZ74945.1,
RC ECO:0000313|Proteomes:UP000076268};
RA Choi J.K., Shah M., Yee N.;
RT "Anaerosporomusa subterraneum gen. nov., sp. nov., a spore-forming obligate
RT anaerobe isolated from saprolite.";
RL Submitted (FEB-2016) 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}.
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:KYZ74945.1}.
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DR EMBL; LSGP01000026; KYZ74945.1; -; Genomic_DNA.
DR RefSeq; WP_066245442.1; NZ_LSGP01000026.1.
DR AlphaFoldDB; A0A154BM03; -.
DR STRING; 1794912.AXX12_15305; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000076268; Unassembled WGS sequence.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000076268}.
FT DOMAIN 471..559
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 561 AA; 59638 MW; 631D1327C9CF6E72 CRC64;
MKKILVIGGV AAGLKAAAKA RRCDSQASIT VLERGKIISY GACGMPYYVG GDVNDIDDLM
KTPVGVLRSP GYFKNAKDIT VLTQTEAMAI DRDSKVVTVK NLATGEDDTL PYDKLVIATG
ASAIKPSLPG VELGNIYSLW HPDDAKAIRQ GIEAGKFNRA IIIGAGLVGM EMAEALTKQQ
LQVTVVEMKD QVFPAFLDPE IAGVVSKYAA EKGINLLAAE KVEAFIGETE VTAVKTDKRT
IPADLVVLAI GARPNVELAR AAGLTIGTTG AISVDDEMRT SDPDIYAGGD CVENINIMSG
QKVFAPMGST ANKHGRVIGE NLCGGHVKFK GVLNTVIAKV HSLTVGKTGL SERDAKQLGY
DYITVMVAGP DKPHYMGAKS ITIKLIADAN TRKVLGMQAV GEGEVAKRVD VAAAVLTMGG
TIDDLFDIDL SYAPPYNSPI DNLAVAANAV MNKLAGKFNG ISPITAKEKM QTGKAVFLDV
RTPDECKQIR LADCPNIKYI PLGQLRSRLA ELNKADEIVA FCKISLRGYE AEGFLEGAGF
ENVKVLEGGI VSWPFACEKE E
//
