ID A0LCU2_MAGMM Unreviewed; 473 AA.
AC A0LCU2;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ABK45785.1};
GN OrderedLocusNames=Mmc1_3296 {ECO:0000313|EMBL:ABK45785.1};
OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetococcus.
OX NCBI_TaxID=156889 {ECO:0000313|EMBL:ABK45785.1, ECO:0000313|Proteomes:UP000002586};
RN [1] {ECO:0000313|Proteomes:UP000002586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1
RC {ECO:0000313|Proteomes:UP000002586};
RX PubMed=19465526; DOI=10.1128/AEM.02874-08;
RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT coccus strain MC-1.";
RL Appl. Environ. Microbiol. 75:4835-4852(2009).
RN [2] {ECO:0000313|EMBL:ABK45785.1, ECO:0000313|Proteomes:UP000002586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1
RC {ECO:0000313|Proteomes:UP000002586};
RX PubMed=22581902;
RA Bazylinski D.A., Williams T.J., Lefevre C.T., Berg R.J., Zhang C.L.,
RA Bowser S.S., Dean A.J., Beveridge T.J.;
RT "Magnetococcus marinus gen. nov., sp. nov., a marine, magnetotactic
RT bacterium that represents a novel lineage (Magnetococcaceae fam. nov.;
RT Magnetococcales ord. nov.) at the base of the Alphaproteobacteria.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP000471; ABK45785.1; -; Genomic_DNA.
DR RefSeq; WP_011714844.1; NC_008576.1.
DR AlphaFoldDB; A0LCU2; -.
DR STRING; 156889.Mmc1_3296; -.
DR KEGG; mgm:Mmc1_3296; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_5; -.
DR OrthoDB; 9809290at2; -.
DR Proteomes; UP000002586; 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; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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; IPR016167; FAD-bd_PCMH_sub1.
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; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR PANTHER; PTHR42934:SF2; GLYCOLATE OXIDASE SUBUNIT GLCD; 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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Reference proteome {ECO:0000313|Proteomes:UP000002586}.
FT DOMAIN 44..223
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 473 AA; 50270 MW; E2EDEDD7785F99DE CRC64;
MNTKGAPHSG SMAVLTALQA RLGAHKVLRD GAHLESYAWD NTGLYARPDG VVLASTLHDV
QTTLALCHAH RVAVTPRTAG TGNVGGALAV EGGIVLSLQR MNRILEINPA DRLVVVEPGV
VNADLQDQLS AHGLFWPPNP SSSKSCAIGG NLAMCAAGPN AVRYGVVRDW VLGLELVTAE
GKVMRTGSRC SKSVTGYDMT RLLVGSEGTL GVITQAILKL TPKPAVQLTM RVVYASVTAA
AQAVSAIMAA GVPPSALEFM DSSCLGLLRQ AGMAIPAQGA ALLLLEVADE VTRVEGEVAR
LQEILQRYAP LELVVARQAA QAKAVWAARY ALSPLLKNLA PKRVNEDVAV PVSRLPELIE
GLQRIAERVD LPIVNFGHAG NGNIHVNLLV DPEDSVVMAR LPDALDRVFD LVVKLDGTLS
GEHGIGYQKR DYLGWELDAE NLAMQRRLKA LFDPNGILNP GKLFSPKPRA TLV
//
