ID C2ERF2_9LACO Unreviewed; 446 AA.
AC C2ERF2;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:EEJ41512.1};
DE EC=1.6.99.3 {ECO:0000313|EMBL:EEJ41512.1};
GN Name=nox {ECO:0000313|EMBL:EEJ41512.1};
GN ORFNames=HMPREF0549_0038 {ECO:0000313|EMBL:EEJ41512.1};
OS Limosilactobacillus vaginalis DSM 5837 = ATCC 49540.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1423814 {ECO:0000313|EMBL:EEJ41512.1, ECO:0000313|Proteomes:UP000004483};
RN [1] {ECO:0000313|EMBL:EEJ41512.1, ECO:0000313|Proteomes:UP000004483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49540 {ECO:0000313|EMBL:EEJ41512.1,
RC ECO:0000313|Proteomes:UP000004483};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) 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:EEJ41512.1}.
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DR EMBL; ACGV01000005; EEJ41512.1; -; Genomic_DNA.
DR RefSeq; WP_003717801.1; NZ_GG693416.1.
DR AlphaFoldDB; C2ERF2; -.
DR STRING; 1423814.HMPREF0549_0038; -.
DR PATRIC; fig|1423814.6.peg.699; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_0_9; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000004483; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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 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.
PE 3: Inferred from homology;
KW Oxidation {ECO:0000256|ARBA:ARBA00023097};
KW Oxidoreductase {ECO:0000313|EMBL:EEJ41512.1}.
FT DOMAIN 1..304
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 333..427
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 446 AA; 49184 MW; EF0A24AE5378B8BD CRC64;
MKVIIVGCTH AGTITATQIL KNHPETEVTI YERNDNVSFL SCGIAVYLSG DVGDPDAMFY
SSPEQLSQLG ADVHMQHNVT SIDPKTKTVK VTDLVTGEEK TDHYDKLVMT TGSWPIIPPI
EGVDSDHVYL CKNYHHAKEL FAAAKDAQRV VVIGAGYIGV ELVEAYTRQN KDVTLVDSAP
RMLHKYFDQE YTDRIQQQFK QKGATLAFNQ RVTGFKDYGD GVTVETDKGS YDADIAILCV
GFRPNTNLLK GKVEMHDNGA IITNEYMQSS DPDIYAAGDS TSVHYNPTGK DAYIPLATNA
IRQGTMAGVN IFGNQMRDMG TQSSSGLNLY GTTMASSGLT LENAKEADID ADSVTIEDNY
RPEFMPTTEK VLMTLVWDKK TRQIIGGQLM SKYDVAQSAG VLSLCIQDKH TIDYLAFVDM
LFQPNFDRPF NYLNILAQAA VAKANK
//
