ID A0A087ASL0_9BIFI Unreviewed; 562 AA.
AC A0A087ASL0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase family protein {ECO:0000313|EMBL:KFI61760.1};
DE EC=1.8.1.14 {ECO:0000313|EMBL:KFI61760.1};
GN ORFNames=BIGA_0283 {ECO:0000313|EMBL:KFI61760.1};
OS Bifidobacterium pullorum subsp. gallinarum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=78344 {ECO:0000313|EMBL:KFI61760.1, ECO:0000313|Proteomes:UP000029046};
RN [1] {ECO:0000313|EMBL:KFI61760.1, ECO:0000313|Proteomes:UP000029046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11586 {ECO:0000313|EMBL:KFI61760.1,
RC ECO:0000313|Proteomes:UP000029046};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KFI61760.1}.
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DR EMBL; JGYX01000001; KFI61760.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087ASL0; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR Proteomes; UP000029046; Unassembled WGS sequence.
DR GO; GO:0050451; F:CoA-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; 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; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR43031:SF1; PHAGE SHOCK PROTEIN E-RELATED PROTEIN; 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; 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; 2.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:KFI61760.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029046}.
FT DOMAIN 144..172
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 460..544
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 562 AA; 60275 MW; C6F7630AA1B5E7B3 CRC64;
MKVVIIGGVA AGATAATRLR RLDERAEIVM LDKGPHVSFS NCSLPFRLSG TVDSTGKLVM
MTPQAFAARY RIGARVNSEA VAIDRDSRTV RVRNLTDGTE YDESYDKLIL SPGARAIVPP
IPGVDQADVF TLKTVTDVDR LHTFLTERGV TRVSVVGGGF IGVEAAVNLV EAGYQVSLVE
AAPQILNTFD QDMVQILHKA LLDHGVNLIV GDQVTRCEGN DLTLASGRVI EGQAVVMAVG
IRPDTALAAD AGLDVNGRGA ILTDASYRTN DPDIYAIGDA IEVTNALTHR PMMLQLAGPA
QKQARQVADH ICGRAVRNTG YIGSNCIKVF EWNAAGTGLT AAQCEREGLR YDYAYVIPQD
KVSLMPDSRP LHVKLIFEVP TGRVLGAQAI GQGDAAKRID VVATAIKFGA VVDDLRDLEL
CYAPPFSNAK DPVNVAALVA GNLLGGDYRQ THVDQARALV ESGATIIDVR EPGAFAKGHL
KGAVNIPLTQ MRGRLDEIPT DRPVYLNCRS SQTSYNAVRL LQGHGFTNVV NLGGSMLGIS
LYEYFTDVTT GREPIVTAYC FD
//
