ID YR135_MIMIV Reviewed; 702 AA.
AC Q5UPL2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Putative GMC-type oxidoreductase R135;
DE EC=1.-.-.-;
GN OrderedLocusNames=MIMI_R135;
OS Acanthamoeba polyphaga mimivirus (APMV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Megamimivirinae; Mimivirus;
OC Mimivirus bradfordmassiliense.
OX NCBI_TaxID=212035;
OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rowbotham-Bradford;
RX PubMed=15486256; DOI=10.1126/science.1101485;
RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA La Scola B., Susan M., Claverie J.-M.;
RT "The 1.2-megabase genome sequence of Mimivirus.";
RL Science 306:1344-1350(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR
RP LOCATION.
RX PubMed=16971431; DOI=10.1128/jvi.00940-06;
RA Renesto P., Abergel C., Decloquement P., Moinier D., Azza S., Ogata H.,
RA Fourquet P., Gorvel J.-P., Claverie J.-M., Raoult D.;
RT "Mimivirus giant particles incorporate a large fraction of anonymous and
RT unique gene products.";
RL J. Virol. 80:11678-11685(2006).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- INTERACTION:
CC Q5UPL2; Q5UPL2: MIMI_R135; NbExp=2; IntAct=EBI-16157702, EBI-16157702;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16971431}. Host
CC membrane {ECO:0000269|PubMed:16971431}; Single-pass membrane protein
CC {ECO:0000269|PubMed:16971431}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AY653733; AAV50410.1; -; Genomic_DNA.
DR RefSeq; YP_003986627.1; NC_014649.1.
DR PDB; 4Z24; X-ray; 2.00 A; A/B=51-702.
DR PDB; 4Z25; X-ray; 3.34 A; A/B/C/D/E/F/G/H/I/J/K/L=51-702.
DR PDB; 4Z26; X-ray; 2.92 A; A/B/C/D/E/F/G/H=51-702.
DR PDB; 7YX3; EM; 4.00 A; A/B=1-702.
DR PDBsum; 4Z24; -.
DR PDBsum; 4Z25; -.
DR PDBsum; 4Z26; -.
DR PDBsum; 7YX3; -.
DR SMR; Q5UPL2; -.
DR DIP; DIP-61553N; -.
DR GeneID; 9924735; -.
DR KEGG; vg:9924735; -.
DR OrthoDB; 2191at10239; -.
DR Proteomes; UP000001134; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Host membrane; Membrane; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix; Virion.
FT CHAIN 1..702
FT /note="Putative GMC-type oxidoreductase R135"
FT /id="PRO_0000243955"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 628
FT /evidence="ECO:0000250"
FT BINDING 58..88
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:4Z24"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:4Z24"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:4Z24"
FT TURN 133..137
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 177..191
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 201..220
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 282..286
FT /evidence="ECO:0007829|PDB:4Z24"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 312..319
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 322..329
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 335..346
FT /evidence="ECO:0007829|PDB:4Z24"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 353..359
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 365..370
FT /evidence="ECO:0007829|PDB:4Z24"
FT TURN 381..384
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 385..388
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 391..401
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 403..409
FT /evidence="ECO:0007829|PDB:4Z24"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:4Z24"
FT TURN 417..421
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:4Z24"
FT TURN 439..443
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 449..456
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 461..467
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 476..483
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 490..493
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 521..531
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 533..558
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 563..570
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 572..585
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 586..593
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 595..598
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 603..615
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 617..621
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 622..625
FT /evidence="ECO:0007829|PDB:4Z24"
FT TURN 635..637
FT /evidence="ECO:0007829|PDB:4Z24"
FT STRAND 643..645
FT /evidence="ECO:0007829|PDB:4Z25"
FT STRAND 649..653
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 656..658
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 668..683
FT /evidence="ECO:0007829|PDB:4Z24"
FT HELIX 687..690
FT /evidence="ECO:0007829|PDB:4Z24"
SQ SEQUENCE 702 AA; 76947 MW; E57AD7FE70F2292B CRC64;
MKNKECCKCY NPCEKICVNY STTDVAFERP NPCKPIPCKP TPIPCDPCHN TKDNLTGDIV
IIGAGAAGSL LAHYLARFSN MKIILLEAGH SHFNDPVVTD PMGFFGKYNP PNENISMSQN
PSYSWQGAQE PNTGAYGNRP IIAHGMGFGG STMINRLNLV VGGRTVFDND WPVGWKYDDV
KNYFRRVLVD INPVRDNTKA SITSVALDAL RIIAEQQIAS GEPVDFLLNK ATGNVPNVEK
TTPDAVPLNL NDYEGVNSVV AFSSFYMGVN QLSDGNYIRK YAGNTYLNRN YVDENGRGIG
KFSGLRVVSD AVVDRIIFKG NRAVGVNYID REGIMHYVKV NKEVVVTSGA FYTPTILQRS
GIGDFTYLSS IGVKNLVYNN PLVGTGLKNH YSPVTITRVH GEPSEVSRFL SNMAANPTNM
GFKGLAELGF HRLDPNKPAN ANTVTYRKYQ LMMTAGVGIP AEQQYLSGLS PSSNNLFTLI
ADDIRFAPEG YIKIGTPNIP RDVPKIFFNT FVTYTPTSAP ADQQWPIAQK TLAPLISALL
GYDIIYQTLM SMNQTARDSG FQVSLEMVYP LNDLIYKLHN GLATYGANWW HYFVPTLVGD
DTPAGREFAD TLSKLSYYPR VGAHLDSHQG CSCSIGRTVD SNLKVIGTQN VRVADLSAAA
FPPGGNTWAT ASMIGARAVD LILGFPYLRD LPVNDVPILN VN
//
