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Database: UniProt
Entry: A0A158NUV0_ATTCE
LinkDB: A0A158NUV0_ATTCE
Original site: A0A158NUV0_ATTCE 
ID   A0A158NUV0_ATTCE        Unreviewed;       603 AA.
AC   A0A158NUV0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=105624558 {ECO:0000313|EnsemblMetazoa:XP_012061308.1};
OS   Atta cephalotes (Leafcutter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Atta.
OX   NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012061308.1, ECO:0000313|Proteomes:UP000005205};
RN   [1] {ECO:0000313|Proteomes:UP000005205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA   Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA   Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA   Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA   Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA   Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA   Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA   Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA   Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA   Weinstock G.M., Gerardo N.M., Currie C.R.;
RT   "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT   insights into its obligate symbiotic lifestyle.";
RL   PLoS Genet. 7:e1002007-e1002007(2011).
RN   [2] {ECO:0000313|EnsemblMetazoa:XP_012061308.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (APR-2016) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; ADTU01026685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012061308.1; XM_012205918.1.
DR   AlphaFoldDB; A0A158NUV0; -.
DR   STRING; 12957.A0A158NUV0; -.
DR   EnsemblMetazoa; XM_012205918.1; XP_012061308.1; LOC105624558.
DR   GeneID; 105624558; -.
DR   KEGG; acep:105624558; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   InParanoid; A0A158NUV0; -.
DR   OrthoDB; 3382025at2759; -.
DR   Proteomes; UP000005205; 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; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF208; RE36204P-RELATED; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005205};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..603
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007629620"
FT   DOMAIN          42..335
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          446..590
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   ACT_SITE        534
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        578
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         127
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         259
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   603 AA;  68287 MW;  D79814391109801D CRC64;
     MKTLWLFIII VTTSSAHNFL DIVKNYIHSP EKDEKFTSNS KYDFIIIGAG SAGSVLANRL
     SENKKWRILL LEAGYMPNFF NRIPIFVGYF QLTGYNWGYN IEPQKNACLG MKNRQCSWPR
     GRGLGGTSIL NYMIHTRGNK FDYDQWASLG NGGWSYVDVL PYFKKSERFN VPGFKNSSYH
     NENGNLCVEH VPYHTKLATT FLNAGQELGY KIVDYNGQDQ KGFSYIQVNI NHGKRCTGAT
     AYLEQINRPN LEIITGARVT KILIDADKRA YGVEYIKDTI WKNVTCSKEV LLSAGTIDSA
     KLLMLSGIGP KEHLEELNIP VIQDSKVGYN MYEHIGFLGL TFMVNQSESL LQSRLFNPKL
     FLEYLLYKRG PISIPGGAEA LAFIRTKYAP DERPDVELLF VSGSLHSDNG QVLKRALRLS
     EDLYDAIYKP IEEQDAWSIW PIVQYPRSVG RLTLRSKDPF EPPKMDPNFF SHPADIEIIL
     EGIKHAINIS KTKAFQAYGS RLHDLKIPGC KQFEFASDDY WRCAIKHLPS MMNHEIGTVK
     MGPQTDTYAV VDPQLKVYGI KTLRVVDASI MPAIPSGHVN AGIYMIGEKA ADMIKQSWKG
     ELY
//
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