ID I0AGT4_IGNAJ Unreviewed; 491 AA.
AC I0AGT4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=FAD/FMN-containing dehydrogenase {ECO:0000313|EMBL:AFH48191.1};
GN OrderedLocusNames=IALB_0479 {ECO:0000313|EMBL:AFH48191.1};
OS Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 /
OS Mat9-16).
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Ignavibacteriaceae; Ignavibacterium.
OX NCBI_TaxID=945713 {ECO:0000313|EMBL:AFH48191.1, ECO:0000313|Proteomes:UP000007394};
RN [1] {ECO:0000313|EMBL:AFH48191.1, ECO:0000313|Proteomes:UP000007394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16
RC {ECO:0000313|Proteomes:UP000007394};
RX PubMed=22661972; DOI=10.3389/fmicb.2012.00185;
RA Liu Z., Frigaard N.-U., Vogl K., Iino T., Ohkuma M., Overmann J.,
RA Bryant D.A.;
RT "Complete genome of Ignavibacterium album, a metabolically versatile,
RT flagellated, facultative anaerobe from the phylum Chlorobi.";
RL Front. Microbiol. 3:185-185(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003418; AFH48191.1; -; Genomic_DNA.
DR RefSeq; WP_014559349.1; NC_017464.1.
DR AlphaFoldDB; I0AGT4; -.
DR STRING; 945713.IALB_0479; -.
DR GeneID; 78242223; -.
DR KEGG; ial:IALB_0479; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_10; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000007394; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 1.
DR Pfam; PF02913; FAD-oxidase_C; 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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007394}.
FT DOMAIN 20..232
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 491 AA; 55794 MW; CEB0CB73FF3EDB47 CRC64;
MIIKTKQDEL QNYLTDASNY KGSCEAVYIP QNKEELIKIL KEANEQRTKV TIAGAGTGLT
GARVPEEGIV ISTEKLNRIL EINIEEKFAI VEPAVYLSHF LDELKSFGFF YPPDPTEKNC
FIGGTVATNA SGAKTFKYGA TRNFVQELEI VLADGNEIYL KRGEVSAKGN KLNLRTKSGK
EIFIELPEIN LPVTKNASGY FVKPNMDAID LFIGSEGTLG VFTKIKLKIL PSPERIISMV
AFFNKEIDAI SFVNKAREIS YRTRQDNLSD EIDALALEFF DNNSLKFLSF DFPNIPPKAN
AAVWFEQEVK LSAEDKLIEK WFSLISDYNV DEEKIWFATN ESERKQIEEF RHAISWKVNE
YISRNNFRKL GTDVAVPDNE MKNFYHFLID LMSKSNLDFV LYGHLGNSHF HLNILPKNEN
EFQSGKELYR KICLKAIELK GTVSAEHGIG KIKTQYLIDM FGEETINKMK AIKQKLDPNY
ILGVGNIFKS S
//
