ID   Y2280_MYCTU             Reviewed;         459 AA.
AC   P9WIT1; L0TBU2; Q50685; Q7D7C5;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Uncharacterized FAD-linked oxidoreductase Rv2280;
DE            EC=1.-.-.-;
GN   OrderedLocusNames=Rv2280;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   PUPYLATION AT LYS-354, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA   Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA   Gygi S.P., Darwin K.H.;
RT   "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT   tuberculosis.";
RL   PLoS ONE 5:E8589-E8589(2010).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- INTERACTION:
CC       P9WIT1; Q80XK6: Atg2b; Xeno; NbExp=3; IntAct=EBI-25767539, EBI-11566520;
CC   -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP45062.1; -; Genomic_DNA.
DR   PIR; D70731; D70731.
DR   RefSeq; WP_003411690.1; NZ_NVQJ01000012.1.
DR   AlphaFoldDB; P9WIT1; -.
DR   IntAct; P9WIT1; 16.
DR   MINT; P9WIT1; -.
DR   STRING; 83332.Rv2280; -.
DR   PaxDb; P9WIT1; -.
DR   TubercuList; Rv2280; -.
DR   eggNOG; COG0277; Bacteria.
DR   OMA; RACNAYS; -.
DR   PhylomeDB; P9WIT1; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.45.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR004113; FAD-linked_oxidase_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; SSF55103; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Isopeptide bond; Oxidoreductase; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..459
FT                   /note="Uncharacterized FAD-linked oxidoreductase Rv2280"
FT                   /id="PRO_0000395888"
FT   DOMAIN          35..214
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT   REGION          28..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        354
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-Cter in protein Pup)"
FT                   /evidence="ECO:0000269|PubMed:20066036"
SQ   SEQUENCE   459 AA;  48052 MW;  5301BAD1396B4B0F CRC64;
     MSEMTARFSE IVGNANLLTG DAIPEDYAHD EELTGPPQKP AYAAKPATPE EVAQLLKAAS
     ENGVPVTARG SGCGLSGAAR PVEGGLLISF DRMNKVLEVD TANQVAVVQP GVALTDLDAA
     TADTGLRYTV YPGELSSSVG GNVGTNAGGM RAVKYGVARH NVLGLQAVLP TGEIIRTGGR
     MAKVSTGYDL TQLIIGSEGT LALVTEVIVK LHPRLDHNAS VLAPFADFDQ VMAAVPKILA
     SGLAPDILEY IDNTSMAALI STQNLELGIP DQIRDSCEAY LLVALENRIA DRLFEDIQTV
     GEMLMELGAV DAYVLEGGSA RKLIEAREKA FWAAKALGAD DIIDTVVPRA SMPKFLSTAR
     GLAAAADGAA VGCGHAGDGN VHMAIACKDP EKKKKLMTDI FALAMELGGA ISGEHGVGRA
     KTGYFLELED PVKISLMRRI KQSFDPAGIL NPGVVFGDT