ID Q988P2_RHILO Unreviewed; 499 AA.
AC Q988P2;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=Mlr6655 protein {ECO:0000313|EMBL:BAB52905.1};
GN OrderedLocusNames=mlr6655 {ECO:0000313|EMBL:BAB52905.1};
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB52905.1, ECO:0000313|Proteomes:UP000000552};
RN [1] {ECO:0000313|EMBL:BAB52905.1, ECO:0000313|Proteomes:UP000000552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC {ECO:0000313|Proteomes:UP000000552};
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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; BA000012; BAB52905.1; -; Genomic_DNA.
DR AlphaFoldDB; Q988P2; -.
DR KEGG; mlo:mlr6655; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_008878_4_2_5; -.
DR Proteomes; UP000000552; Chromosome.
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; 3.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 114..300
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 433..492
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 499 AA; 54538 MW; 633924AED96B8F51 CRC64;
MMEHTADIVI IGSGIGGSSL AYSLADTGRR IVILERGEHL RDTPEARDDI AIFQNGFYRS
SEEWLATDGE SFLPGNYYYV GGNSKFFGAV MYRYRQEDFN PRDHMGGRSP GWPISYAELE
PWYERAEILF GVRGDARQDP TEPPRNRPYR YLPVPDEPAI ATVRQRLLQA GIHPASLPLA
IDIDAWLRRA KTGWDAFPNT GAGKIDAEVG PLTKALEHPN ATLITGANVQ RLVTDASGRR
VMAAVFIKDG VELSIGADVF AVAAGAVQSA ALLLRSSTSV YPNGLGNSSD QLGRNFMNHN
TTAMLAIDPF RRNTAVYQKT LGFNDFYNKD PLGSFPLGNV QLLGHITGNI LKANAPLLPR
WLAGLVARNC YGWFLTSEDL PNPESRVTIR NGRIVMNWVR NNMGAHETLI RRTRAVMREA
GFPVVLTRTF GRKTTSHQCG TARLGSDPNT SVVSPDCRSH DIANLYVTDA SVLPTSAAVN
PALTIAALAL KAGAAIRAM
//
