ID A0A022KXI7_9MICO Unreviewed; 472 AA.
AC A0A022KXI7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:EYT47751.1};
GN ORFNames=D641_0114540 {ECO:0000313|EMBL:EYT47751.1};
OS Brachybacterium muris UCD-AY4.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=1249481 {ECO:0000313|EMBL:EYT47751.1, ECO:0000313|Proteomes:UP000019754};
RN [1] {ECO:0000313|EMBL:EYT47751.1, ECO:0000313|Proteomes:UP000019754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-AY4 {ECO:0000313|EMBL:EYT47751.1,
RC ECO:0000313|Proteomes:UP000019754};
RX PubMed=23516213;
RA Lo J.R., Lang J.M., Darling A.E., Eisen J.A., Coil D.A.;
RT "Draft genome sequence of an Actinobacterium, Brachybacterium muris strain
RT UCD-AY4.";
RL Genome Announc. 1:E0008613-E0008613(2013).
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}.
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:EYT47751.1}.
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; AORC01000024; EYT47751.1; -; Genomic_DNA.
DR RefSeq; WP_031307297.1; NZ_AORC01000024.1.
DR AlphaFoldDB; A0A022KXI7; -.
DR STRING; 1249481.D641_0114540; -.
DR HOGENOM; CLU_018354_10_0_11; -.
DR OrthoDB; 9775082at2; -.
DR Proteomes; UP000019754; Unassembled WGS sequence.
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; 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 PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000019754}.
FT DOMAIN 47..217
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 472 AA; 51927 MW; 895F51E671482E7E CRC64;
MATTTNRHPV PEAQPALARM RKHLAGPLIE PPDAGYDQAR AVWNGMVDRY PLAIARAATV
DDVPIVLEAA RETGLPLAVR GGGHSITGLS TVDDGIVLDL GDLREVVVDP ATQLVTVAPG
ARSADVDAAT APHRLAIPLG ASSLPGVAGL TLGGGVGWLT RRAGLALDCL ERAEVVNAQG
EHLVASREDH PDLFWGLRGG GGNFGVVTSF TFRAVRLPQT VLGWTLVYAP SQWWHALAAF
ERWARELPDE LSSILTFRAM PEVSGMGEET CLMIRCVYVG EDPARGTAML DRLRRTAPPV
HETSGPISWP QWQSVMDAHF PFGSHGFWRN VAFTRMDEDA LGAVLDVAER IPGPGHAIDI
HHLGGAFARV PEQATAFPNR TARFWMNIYG AWQESEEDSR GWDLAGHSRV VMERLAERGE
YVNFRALEYT RPITDFTRHI YGEEKYRRLQ RVKQRYDPQN LFRGNYNVSP DV
//
