ID H5XBZ4_9PSEU Unreviewed; 457 AA.
AC H5XBZ4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=FAD/FMN-dependent dehydrogenase {ECO:0000313|EMBL:EHR52781.1};
GN ORFNames=SacmaDRAFT_4598 {ECO:0000313|EMBL:EHR52781.1};
OS Saccharomonospora marina XMU15.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharomonospora.
OX NCBI_TaxID=882083 {ECO:0000313|EMBL:EHR52781.1, ECO:0000313|Proteomes:UP000004926};
RN [1] {ECO:0000313|EMBL:EHR52781.1, ECO:0000313|Proteomes:UP000004926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XMU15 {ECO:0000313|EMBL:EHR52781.1,
RC ECO:0000313|Proteomes:UP000004926};
RX PubMed=22768369; DOI=10.4056/sigs.2655905;
RA Klenk H.P., Lu M., Lucas S., Lapidus A., Copeland A., Pitluck S.,
RA Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G., Land M.,
RA Ivanova N., Rohde M., Goker M., Detter J.C., Li W.J., Kyrpides N.C.,
RA Woyke T.;
RT "Genome sequence of the ocean sediment bacterium Saccharomonospora marina
RT type strain (XMU15(T)).";
RL Stand. Genomic Sci. 6:265-275(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; CM001439; EHR52781.1; -; Genomic_DNA.
DR RefSeq; WP_009156159.1; NZ_CM001439.1.
DR AlphaFoldDB; H5XBZ4; -.
DR STRING; 882083.SacmaDRAFT_4598; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_018354_10_0_11; -.
DR OrthoDB; 9775082at2; -.
DR Proteomes; UP000004926; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000004926}.
FT DOMAIN 32..202
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 457 AA; 49378 MW; D7816FAFE5C162EF CRC64;
MTRSLSDSIA GAVIGPDDPE YAEARKVWNG DIDRRPALIV RCASVSDVVA AIRYAREEAL
EIAVRGGGHS TPGMSAVDDG LVIDLSDINS VEVDPTTKRA RVGAGARLAE LDAATQEHGL
AVPTGLISHT GIAGLTLGGG MGWLTRQAGL TIDNLVSAEM VTADGSVLRV SENENPELFW
AIRGGGGNFG VVTEFELALH DVGPTIQFGF LFWDVEQGPE LLRLARDTIA ALPRELNIVV
AGLSAPAAEF VPEQYHLRTG YALMVAGFGS PETHSEIVDA LRAALPPLFD FTAPMPYVAL
QQLLDEGSPW GTLCYEKSLY LEDLSDEVIS TVCEQLPRKS SANSMLTLYR LDEEYSRPAD
EDTAFSGSRK PQYAAFVVGM CPTAELLATE RVWVRSFWEA LTPHIAATGT YVNAIGKSTD
DRVRAAYGTE KYERLAKLKS LYDPHNVFHR NANIKPA
//
