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Database: UniProt
Entry: A0A0M2CUP6_9MICC
LinkDB: A0A0M2CUP6_9MICC
Original site: A0A0M2CUP6_9MICC 
ID   A0A0M2CUP6_9MICC        Unreviewed;       473 AA.
AC   A0A0M2CUP6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:EYT52315.1};
GN   ORFNames=H488_0109195 {ECO:0000313|EMBL:EYT52315.1};
OS   Kocuria sp. UCD-OTCP.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=1292021 {ECO:0000313|EMBL:EYT52315.1, ECO:0000313|Proteomes:UP000033173};
RN   [1] {ECO:0000313|EMBL:EYT52315.1, ECO:0000313|Proteomes:UP000033173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-OTCP {ECO:0000313|EMBL:EYT52315.1,
RC   ECO:0000313|Proteomes:UP000033173};
RX   PubMed=23661474;
RA   Coil D.A., Doctor J.I., Lang J.M., Darling A.E., Eisen J.A.;
RT   "Draft Genome Sequence of Kocuria sp. Strain UCD-OTCP (Phylum
RT   Actinobacteria).";
RL   Genome Announc. 1:E00172-13(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:EYT52315.1}.
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DR   EMBL; AOSQ01000018; EYT52315.1; -; Genomic_DNA.
DR   RefSeq; WP_017832960.1; NZ_AOSQ01000018.1.
DR   AlphaFoldDB; A0A0M2CUP6; -.
DR   HOGENOM; CLU_018354_10_0_11; -.
DR   Proteomes; UP000033173; 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;
FT   DOMAIN          47..217
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   473 AA;  51531 MW;  42725C0CACDDDFA7 CRC64;
     MNAVDRGEHD QEIARELEKL RTHLTGTLVE PDDPLYDEAR RVWNGMVDVR PRAVVQAGAV
     SDIDPVLAAA QHTDLPLAVR GGGHNVAGHG TVEGGLVLDL GALRRVEVDP ETRRVTVEPG
     ATLADVDRAT VPHGLAVPLG VVSATGVAGL TVGGGVGWLT RSNGLSLDNL VDAEVITGTR
     EHLHANAEHN PDLFWGIRGG GGNFGIVTSF TFRARELPAS VLGGNLIYGR EHWRTALQAF
     ARWTDDLPDE MNGIVSILRF PPSFGMGDEP WLIIGFAWMS PDHAEGLRLV DRLRADAPPD
     EEEVGPVQWT EWQSAMDELF PKGARGYWKN ASFSRLDDEV VDALLGAASE ITWFGTGIDI
     HHMEGFCGRV PAGATAFPNR SARYWLNVYG YWPDAADDAR LTAFARKAHA AVEPFADAGL
     YVNFLGAEHG PVTPETARQA YGERTHRRLV ELKNRYDPGN LFRLNHNILP NVA
//
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