ID Q7APS7_MYCLE Unreviewed; 449 AA.
AC Q7APS7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Possible oxidoreductase {ECO:0000313|EMBL:CAC32163.1};
GN OrderedLocusNames=ML2631 {ECO:0000313|EMBL:CAC32163.1};
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631 {ECO:0000313|EMBL:CAC32163.1, ECO:0000313|Proteomes:UP000000806};
RN [1] {ECO:0000313|EMBL:CAC32163.1, ECO:0000313|Proteomes:UP000000806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN {ECO:0000313|EMBL:CAC32163.1,
RC ECO:0000313|Proteomes:UP000000806};
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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DR EMBL; AL583926; CAC32163.1; -; Genomic_DNA.
DR PIR; E87238; E87238.
DR RefSeq; NP_302685.1; NC_002677.1.
DR RefSeq; WP_010909004.1; NC_002677.1.
DR AlphaFoldDB; Q7APS7; -.
DR STRING; 272631.gene:17576497; -.
DR KEGG; mle:ML2631; -.
DR PATRIC; fig|272631.5.peg.5051; -.
DR Leproma; ML2631; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_4_1_11; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
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; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000806}.
FT DOMAIN 32..211
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 449 AA; 47158 MW; 9684AFDA32B99E87 CRC64;
MLRSLAAVVG SSHVIADPDV LIAHSIDHTG RYRGQARALV RPGTAEQVTE VLRVCRDVGA
HVTVQGGRTS LVAGTVPEHN DVLLSTERLR SISEVDTVER RLRVGAGATL TAVQNAATAA
GLVFGVDLCA RATATVGGMA STNAGGLRTV RYGNMGEQVI GLEVALPDGS LLCRHSLARF
DNTGYNLPAL FVGAEGTLGV ITALDLRLHP APAHRVTAVC GFSDLGALVD ASRAFRDVYG
IAALELIDGR ASSLIREHLG VSSPVDGDWL LLVELAADHD QTNRLAELSM AVQMCGVPAV
GVDAGAQQRL WRVRESLAEV LGVYGPPLKF DVSLPLSAIS GFAKEAATLI DAQVSDVQEA
LPVLFGHVGE GNLHLNVLRC PPDREKTLTA AMMELIAQAG GNVSSEHGVG SNKRAYLRMS
RDPADIAAMR TIKAALDPTG YLNAAVLFD
//
