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Database: UniProt
Entry: T1J979_STRMM
LinkDB: T1J979_STRMM
Original site: T1J979_STRMM 
ID   T1J979_STRMM            Unreviewed;      2348 AA.
AC   T1J979;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
OS   Strigamia maritima (European centipede) (Geophilus maritimus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Myriapoda; Chilopoda;
OC   Pleurostigmophora; Geophilomorpha; Linotaeniidae; Strigamia.
OX   NCBI_TaxID=126957 {ECO:0000313|EnsemblMetazoa:SMAR010270-PA, ECO:0000313|Proteomes:UP000014500};
RN   [1] {ECO:0000313|Proteomes:UP000014500}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Brora {ECO:0000313|Proteomes:UP000014500};
RA   Richards S.R., Qu J., Jiang H., Jhangiani S.N., Agravi P., Goodspeed R.,
RA   Gross S., Mandapat C., Jackson L., Mathew T., Pu L., Thornton R., Saada N.,
RA   Wilczek-Boney K.B., Lee S., Kovar C., Wu Y., Scherer S.E., Worley K.C.,
RA   Muzny D.M., Gibbs R.;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:SMAR010270-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (FEB-2015) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; JH431970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 126957.T1J979; -.
DR   EnsemblMetazoa; SMAR010270-RA; SMAR010270-PA; SMAR010270.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_229703_0_0_1; -.
DR   OMA; KNNERYH; -.
DR   OrthoDB; 3382025at2759; -.
DR   PhylomeDB; T1J979; -.
DR   Proteomes; UP000014500; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; 6.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 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; 4.
DR   Pfam; PF00732; GMC_oxred_N; 5.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 4.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 5.
DR   PROSITE; PS00623; GMC_OXRED_1; 4.
DR   PROSITE; PS00624; GMC_OXRED_2; 4.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014500}.
FT   DOMAIN          59..82
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          235..249
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   DOMAIN          594..617
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          930..944
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   DOMAIN          1336..1359
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          1511..1525
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   DOMAIN          1906..1929
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          2082..2096
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
SQ   SEQUENCE   2348 AA;  261850 MW;  C7B3DA3B58E71CE2 CRC64;
     GAGAAGAAIA ARLSEKEKFQ VLLLEAGGEP PFFVQIPYLS MGPFGGEYDW SFKWVIPRGK
     GLGGSTLING LVFTRGNKND YDHWQSLGND GWSYNDLLPY FKKLEDYQIP LKPEDEIIHS
     KGGPVTATVS EYKTPLQEII FDAFQETGYS LQDYNGQTQT GYFHNVAVVR NGSRCDAYTS
     YLEPNRNRAN LHIVTHAFVT KVKFDDKNKA VGVYFEKDNK IYFVPAEKEV ILASGSNNSP
     HLLMLSGIGP KEMLEKYKIK PVTDSPGVGG NLQDHATVAG MVFVFDEPIG FDFSCDVHQN
     SFELWHSKRQ GVLTVPIHSE AISFLKTKFA PVDKDWPDFE LQIVQPPAMP DNLKNEYKKP
     FFAQHNSRMM VMLPILMRPK SVGHVRLQSG DPHVPLAIQP NYLSNEDDVN VLLEVVKAGL
     NLTRTQPFAK LGTKWHGQII PGCKMFDELS DDYWKCYIRH YTYGLFHQSG TCKMGSQTDP
     LAVVDSRLRV YGVEGLRVAD VSISPSIITG HTMVPAIMIV GAGASGGALA SRLSEDKNFN
     VLLLEAGGEP QFLNTIPYFA PGPFGGELDW GYQTESQKHA CLALVNEQCP WPQGKGLGGS
     TLINALVYNR ADPSDYDNWE KLGNEGWSYD DVLPYFKKLE DFKGFVDKNN ERYHGFGGPM
     LAARPPYETE LARVIIEAGQ ELGYSEVDYN GQAIRGFMGL KIFGLLISGI STKIGAGASG
     GTLASRLSED KKHNVLLLEA GGEPKFLNTI PYFAPGPFGG DLDWNYETDS QKSACLALQN
     EKWAWPRGKG LGGSTLINGL VFNRCDPNDY DKEYHGFSGP MPAAKPPFKT ELAQVIIEAG
     QELGYSEIDY NAKSTKGFAN PVFILKNGTR YTVYDGYLKE ARKRANLDIL TGALVEKVEF
     DGNTAVGVLF LRDGQTWSVK ARKEIILSAG AVNTPKILML SGIGPKETLT KYEIPVIKHL
     PGVGQNLQDH IAAINTKITL NEDVGFKYLK DIDAANLEKW ETKREGPLTV PLGVEGIAFI
     DSEYSVKTIN WPDLEILFLQ TPLKFNRKKE YELEMIAPNG NNFLFTLIIA LRPKSVGYIT
     IQGKSVYDLP SLQPKYLSDK DDVDLLVSGV KIFQNLTKTK AFQKYQAHWD HDTPTKGCEQ
     YKFLSDEYLA CDIRYHSMGV FHQCCTAKMG PKNDPMAVVD SKLRVHGVKK LRVVDMSIPP
     NVPSGHTMVP SIMIGEKAAD MIKEYSPYYS TIEITAWYQL VLRLSIAINT YAADKSYDFI
     VVGAGASGGA LASRLSEDKN FNVLLLEAGG EPQFLNTIPY FAPGPFGGEL DWNYQTESQK
     HACLALVNEQ CPWPRGKGLG GSTLINALVY NRADPSDYDN WEKLGNEGWS YDDVLPYFKK
     LEDFKGFVDK NNERYHGFGG PMPAARPPYE TELARVIIEA GQELGYSEVD YNGEAIRGFS
     NFMFILKNGS RHSVYDGYIK EARKRANLDI LTGALVEKIE FNDKTAVGVI FQHDGKIWRV
     KAEKEIVLSA GALSSPQILM RSGIGPRDIL SKYEIPVVAN LPGVGQNLQD HIGVINLAIR
     LNEDIGFKLM RDINAGNFEK WERKREGPLT VPVTGEGIAF VDTEYSDKTK NPPDLEMIFY
     QTPLLMNFKE QYKSKLTAPD GQNFMFVILL LLRPKSVGYT AIKGKTALEI PLFQPNFLTD
     KDDIDRLVSG MKMFLNVTKT KAFQKYDAFW DHDAPIKGCE QYEFLSDDYF ACYVGHYSIG
     FFHECCTAKM GPKDDIMAVV NSKLRVYGVK NLRVADMICQ QGERQAQDYH GFSGPMPAAK
     PLFKTELAQV IIEAGQELGY SEIDYNVKST TVGAGASGGA LASRLSEDKN FNVLLLEAGG
     EPEFLNTIPY FAPGPFGGEL DWDYQTESQK HACLALLNEQ CPWPRGKGLG GSTLINSLVY
     NRADPSDYDN WEKLGNEGWS YYDVLPYFKK LEDFKGFVDK NNERYHGFGG PMLAARPPYE
     TELARVIIEA GQELGYSEVD YNGQAIRGFS NGMFILKNGS RHSVYDGYIK EARKRANLDI
     LTGALVEKIE FNDKTEAVGV IFQHDGKIWR VKAEKEIVLS AGALSSPQIL MRSGIGPRDI
     LSKYEIPVVA NLPGVGQNLQ DHIGVINLAI RLNEDIGFKL MRDINAGNFE KWERKREGPL
     TVPVTQEGIA FVDTEYSDKT KNPPDLEMIF YQTPLLMNFK EVICYSITST IQYKSRLTAP
     DGQNFMFLIL LLLRPKSVGY TVIKGKTAHD VPLFQPNFLT DKNDIDRLVS GMKMFLNVTK
     TKAFQKYDAF WDHDTPIKGC EQYEILSDDY LACYAGHYSI GFFHECCTAK MGPKDDTMAV
     VNSKLSVI
//
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