ID Q09BC8_STIAD Unreviewed; 439 AA.
AC Q09BC8;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE SubName: Full=FAD-dependent dehydrogenase {ECO:0000313|EMBL:ADO69069.1};
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:EAU69086.1};
GN OrderedLocusNames=STAUR_1265 {ECO:0000313|EMBL:ADO69069.1};
GN ORFNames=STIAU_8620 {ECO:0000313|EMBL:EAU69086.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU69086.1, ECO:0000313|Proteomes:UP000032702};
RN [1] {ECO:0000313|EMBL:EAU69086.1, ECO:0000313|Proteomes:UP000032702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU69086.1,
RC ECO:0000313|Proteomes:UP000032702};
RA Nierman W.C.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO69069.1, ECO:0000313|Proteomes:UP000001351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO69069.1,
RC ECO:0000313|Proteomes:UP000001351};
RX PubMed=21037205; DOI=10.1093/molbev/msq292;
RA Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA Sogaard-Andersen L.;
RT "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL Mol. Biol. Evol. 28:1083-1097(2011).
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DR EMBL; CP002271; ADO69069.1; -; Genomic_DNA.
DR EMBL; AAMD01000009; EAU69086.1; -; Genomic_DNA.
DR RefSeq; WP_002611249.1; NZ_AAMD01000009.1.
DR STRING; 378806.STAUR_1265; -.
DR KEGG; sur:STAUR_1265; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_032465_0_0_7; -.
DR OMA; YTVAWID; -.
DR OrthoDB; 143770at2; -.
DR Proteomes; UP000001351; Chromosome.
DR Proteomes; UP000032702; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016899; F:oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR010031; FAD_lactone_oxidase-like.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR43762:SF1; D-ARABINONO-1,4-LACTONE OXIDASE; 1.
DR PANTHER; PTHR43762; L-GULONOLACTONE OXIDASE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
FT DOMAIN 1..178
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 439 AA; 49417 MW; 8E04AD27FE9CBEC8 CRC64;
MTNDLQSWGR FPLATRQTPR ALSWQTDAIP ASGTSLLPYG QGRSYGDSCL NENGTLITTH
SLDRLLDFDA ATGVVRCEAG TTLETLLKLT VPRGWFLPVT PGTKFVSVGG AIANDVHGKN
HHRAGTFGRY VRRFELLRSD GSRKVCSPEE NPDWYEATIG GLGLTGLILW ADVQMRPIHN
PFVITETVPM ADLEDFFRIS RESEQDYELT VAWVDSLALG RRLGRGLFFR GNFAPPRFDG
LPLVKSHLSH GSALAVPFNL PGISLNWLSV AVFNWFFYRA NLLRRGPRLQ HYDPFFYPLD
KVHRWNRVYG RKGFFQFQCV VPFSTAREAL REIMERSARD VPSPLTVLKT FGDTPSPGWM
SFPRPGVTLA LDFANRGERT MKLVAELDHL TRQAGGAVYP AKDAGMSPEN FAAYFPQLER
FKSYIDPAFS SSFWRRMNP
//