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Database: UniProt
Entry: A0A090ANT5_9GAMM
LinkDB: A0A090ANT5_9GAMM
Original site: A0A090ANT5_9GAMM 
ID   A0A090ANT5_9GAMM        Unreviewed;       528 AA.
AC   A0A090ANT5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:BAP57120.1};
GN   ORFNames=THII_2823 {ECO:0000313|EMBL:BAP57120.1};
OS   Thioploca ingrica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Thioploca.
OX   NCBI_TaxID=40754 {ECO:0000313|EMBL:BAP57120.1, ECO:0000313|Proteomes:UP000031623};
RN   [1] {ECO:0000313|EMBL:BAP57120.1, ECO:0000313|Proteomes:UP000031623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kojima H., Ogura Y., Yamamoto N., Togashi T., Mori H., Watanabe T.,
RA   Nemoto F., Kurokawa K., Hayashi T., Fukui M.;
RT   "Ecophysiology of Thioploca ingrica as revealed by the complete genome
RT   sequence supplemented with proteomic evidence.";
RL   ISME J. 0:0-0(2014).
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}.
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DR   EMBL; AP014633; BAP57120.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090ANT5; -.
DR   STRING; 40754.THII_2823; -.
DR   KEGG; tig:THII_2823; -.
DR   HOGENOM; CLU_008878_4_1_6; -.
DR   OrthoDB; 9787779at2; -.
DR   Proteomes; UP000031623; Chromosome.
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; 2.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR   PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000031623}.
FT   DOMAIN          17..229
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   DOMAIN          390..517
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   528 AA;  59528 MW;  097FE97841D7AB97 CRC64;
     MINDFREMTN ETVIETDICI VGAGAAGISI AKYLNGSNIS ICLVESGGFK FEEETQSLYQ
     GKNVGHKYFP LDTARLRYFG GTTNHWTGWC SPLEEVDFKQ RDWVPYSGWP FTQKDLEPYY
     IQAQKWCNVG PYRYQPSDWE TDDFKLLEVL PEKLATKFWQ FSPAPTRFGI TYRAELEQAT
     HIQVLLHANV VEILSNSSAQ AVEGVKISTV DKVKTGTVRA KVVILACGGL ENPRLLLVSN
     RVQTTGLGNQ NDNVGRFFME HPLVESGKLI TLKDSKPLAY YNNITIRNGA HLRPALKGSE
     IAQQKYQILN VAVLMHSDSQ NEEIGYLATK KFFKALKSGK FSNQFRNDVI NMISDLDGLA
     ENLYYRFRGT QKPLPNNTNI TVMSYSEQRP NPNSRVLLDT DKDQLGLPRI KLDWQLTELE
     KRSVRVTNQL IGEELGRMEL GRLQLVDWLQ SEDDQFKAGG QYHHMGTTRM SEDPKQGVVD
     KNCRVHGLAN LYIAGSSVFA TSGNSNPTLT IVALAMRLAE HLKKQVVS
//
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