ID D2QW56_PIRSD Unreviewed; 576 AA.
AC D2QW56;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Cyclic nucleotide-regulated FAD-dependent pyridine nucleotide-disulphide oxidoreductase {ECO:0000313|EMBL:ADB15931.1};
DE EC=1.8.1.9 {ECO:0000313|EMBL:ADB15931.1};
GN OrderedLocusNames=Psta_1253 {ECO:0000313|EMBL:ADB15931.1};
OS Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella
OS staleyi).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Pirellula.
OX NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB15931.1, ECO:0000313|Proteomes:UP000001887};
RN [1] {ECO:0000313|EMBL:ADB15931.1, ECO:0000313|Proteomes:UP000001887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128
RC {ECO:0000313|Proteomes:UP000001887};
RX PubMed=21304671; DOI=10.4056/sigs.51657;
RA Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., Lucas S.,
RA Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Pirellula staleyi type strain (ATCC 27377).";
RL Stand. Genomic Sci. 1:308-316(2009).
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DR EMBL; CP001848; ADB15931.1; -; Genomic_DNA.
DR AlphaFoldDB; D2QW56; -.
DR STRING; 530564.Psta_1253; -.
DR KEGG; psl:Psta_1253; -.
DR eggNOG; COG0492; Bacteria.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_031864_5_8_0; -.
DR Proteomes; UP000001887; Chromosome.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR48105:SF5; BLR1248 PROTEIN; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ADB15931.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001887}.
FT DOMAIN 41..160
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
SQ SEQUENCE 576 AA; 62161 MW; DC64F28C05935D8E CRC64;
MGENCGAWMV RGGRWRYDWS VTFVPLRAEA LVKHATPQSI AFPRLSDSQF ELVASMGTRH
TFAPGDFVVQ AGQRGYPLWV IETGEVAIVE STSGITREVV RHTERSFIGD VDILTGRPTV
ISAIATVPTT AIRVDAPLVR PLLCDRPELG EMLLEAIQMR RLLLQQSGFV GSKLIGARYS
KKTQALREFF YKNHVPHTFY DIEEPEGQQE LSQTGASLEE VPVVVCNGKI VKQPVLSKIA
ECLGISRHIQ EDLFDLLVIG SGPAGLAATV YAASEGLKTL VLDRVGPGGQ AGSSSKIENL
IGFPSGISGA DLANRGYLQA LKFGAQFTAP VAVREILRNP DQTFSLELCT GQMARARVVL
LATGVSYDSL ECPGIRELAG TGVYYAATSV EARACHDTTA IIIGGGNSAG QAAMFLAERA
RHVKMVIRAE NLSKGMSSYL STRILSHPKI ELVPSTELVC VSGERSVEQV TLKDCKTNLE
TQHDCSALFI FIGGKPNTDW LMTDVARDEK GFLLTGAMVP RSQWSLARQP FDLETSVPGL
LAAGDVRSGT TKRCGFAVGD GSLAVTCVHR YLASTT
//
