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Database: UniProt
Entry: I0HBX9_ACTM4
LinkDB: I0HBX9_ACTM4
Original site: I0HBX9_ACTM4 
ID   I0HBX9_ACTM4            Unreviewed;       397 AA.
AC   I0HBX9;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Putative FAD-dependent oxidoreductase {ECO:0000313|EMBL:BAL90516.1};
GN   OrderedLocusNames=AMIS_52960 {ECO:0000313|EMBL:BAL90516.1};
OS   Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 /
OS   JCM 3121 / NBRC 102363 / NCIMB 12654 / NRRL B-3342 / UNCC 431).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=512565 {ECO:0000313|EMBL:BAL90516.1, ECO:0000313|Proteomes:UP000007882};
RN   [1] {ECO:0000313|EMBL:BAL90516.1, ECO:0000313|Proteomes:UP000007882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NBRC 102363 /
RC   NCIMB 12654 / NRRL B-3342 / UNCC 431
RC   {ECO:0000313|Proteomes:UP000007882};
RA   Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H.,
RA   Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.;
RT   "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC
RT   102363).";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the L2HGDH family.
CC       {ECO:0000256|ARBA:ARBA00037941}.
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DR   EMBL; AP012319; BAL90516.1; -; Genomic_DNA.
DR   RefSeq; WP_014445404.1; NC_017093.1.
DR   AlphaFoldDB; I0HBX9; -.
DR   STRING; 512565.AMIS_52960; -.
DR   KEGG; ams:AMIS_52960; -.
DR   PATRIC; fig|512565.3.peg.5290; -.
DR   eggNOG; COG0579; Bacteria.
DR   HOGENOM; CLU_024775_0_1_11; -.
DR   OrthoDB; 9801699at2; -.
DR   Proteomes; UP000007882; Chromosome.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR43104; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43104:SF2; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007882}.
FT   DOMAIN          6..392
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   397 AA;  42683 MW;  146BA8D70E2E3088 CRC64;
     MADETIAIIG AGIVGLAIGR EITLRRPGAR VVLLEKEAEV AQHQTGHNSG VVHAGIYYTP
     GSLKAELCTR GRLLLREYCA ERGIAYDECG KLVVAVRADE LGRLDNLEKR ARENGVPGLR
     RVDPAGIREI EPHAAGLAAL HSPETAITDF PGVARAFAAD IGAAGGEVRT GFAVDRLTPQ
     GARIEIAAGE RRLLADRVIV CAGIQSDRVA KLAGDAPGPR IIPFRGEYMR VKPAKADLVR
     GMIYPVPDPR YPFLGVHFTR RVTGVVEVGP NAVLATAKEG YRRTQVNVFD LAGIAAWPGT
     WRMARQHWRT GVKEVLGSLS QRRYMAEAMR YVPEIGAADV ERAGAGVRAQ ALDRDGSLVD
     DFRIHRLGPV TAVRNAPSPA ATSSLAIAEH VVGQIFE
//
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