ID   LODB_MARM1              Reviewed;         369 AA.
AC   F2JXJ2; Q24K53;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Putative FAD-dependent oxidoreductase LodB;
DE            EC=1.-.-.-;
GN   Name=lodB; OrderedLocusNames=Marme_2661;
OS   Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 /
OS   MMB-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=717774;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1;
RX   PubMed=16547036; DOI=10.1128/jb.188.7.2493-2501.2006;
RA   Lucas-Elio P., Gomez D., Solano F., Sanchez-Amat A.;
RT   "The antimicrobial activity of marinocine, synthesized by Marinomonas
RT   mediterranea, is due to hydrogen peroxide generated by its lysine oxidase
RT   activity.";
RL   J. Bacteriol. 188:2493-2501(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1;
RX   PubMed=22675599; DOI=10.4056/sigs.2545743;
RA   Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA   Detter J.C., Copeland A., Teshima H., Bruce D., Detter C., Tapia R.,
RA   Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W.,
RA   Sanchez-Amat A.;
RT   "Complete genome sequence of the melanogenic marine bacterium Marinomonas
RT   mediterranea type strain (MMB-1(T)).";
RL   Stand. Genomic Sci. 6:63-73(2012).
RN   [3]
RP   FUNCTION IN LODA MATURATION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP   AND OPERON STRUCTURE.
RC   STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1;
RX   PubMed=20025674; DOI=10.1111/j.1365-2958.2009.07000.x;
RA   Gomez D., Lucas-Elio P., Solano F., Sanchez-Amat A.;
RT   "Both genes in the Marinomonas mediterranea lodAB operon are required for
RT   the expression of the antimicrobial protein lysine oxidase.";
RL   Mol. Microbiol. 75:462-473(2010).
CC   -!- FUNCTION: Is required for lysine-epsilon oxidase (LOD) activity in
CC       M.mediterranea. May be involved in the generation of the quinonic
CC       cofactor of LodA, leading to the active form of LodA containing a
CC       tyrosine-derived quinone cofactor. {ECO:0000269|PubMed:20025674}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20025674}.
CC   -!- INDUCTION: Forms part of an operon with lodA.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not show any lysine-
CC       epsilon oxidase activity. {ECO:0000269|PubMed:20025674}.
CC   -!- MISCELLANEOUS: The intracellular stability of LodB is dependent on the
CC       presence of LodA protein. {ECO:0000305|PubMed:20025674}.
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DR   EMBL; AY968053; AAY33850.1; -; Genomic_DNA.
DR   EMBL; CP002583; ADZ91892.1; -; Genomic_DNA.
DR   RefSeq; WP_013661795.1; NC_015276.1.
DR   AlphaFoldDB; F2JXJ2; -.
DR   SMR; F2JXJ2; -.
DR   STRING; 717774.Marme_2661; -.
DR   EnsemblBacteria; ADZ91892; ADZ91892; Marme_2661.
DR   KEGG; mme:Marme_2661; -.
DR   PATRIC; fig|717774.3.peg.2747; -.
DR   eggNOG; COG0644; Bacteria.
DR   HOGENOM; CLU_024648_6_2_6; -.
DR   OMA; WCAVGDA; -.
DR   OrthoDB; 1770293at2; -.
DR   Proteomes; UP000001062; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..369
FT                   /note="Putative FAD-dependent oxidoreductase LodB"
FT                   /id="PRO_0000423013"
FT   BINDING         10..14
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   369 AA;  41421 MW;  A4E46B88C3636D57 CRC64;
     MESYDAIVIG GGPAGAASAL SLLTHHNKRV LLLERGDFSQ ARIGEQVSHS IFDFLAYLDL
     PVSEFGESCF SPNYGKTSLW GSSIESHHLS MFATQGATYQ LDRAAFDETL LMAFVERGGT
     VIPRCKQMKI EQSDSVWQVQ FVHPEQGEQT VCCDYLVDAS GRQSKLSAML GVEPVMDDQL
     VGVGAFIRNP DNAFEQHQRI ESCEYGWWYM AGLSSELAVV TCFTDMDIMR EMRLNKASVW
     NQYLAETSAI ADCVKGSETT HPKLWVKQAH SQYCTSELPD RFIAVGDAAL SFDPVSSMGI
     GFAMTSACHS TRALVSDSKD AVLQYQQDMA RIYQEYHVTK TRIYQREKRW PNQLFWQRRH
     AFSALQHAS