LOCUS WP_035229192 522 aa linear BCT 27-MAR-2023
DEFINITION MULTISPECIES: GMC family oxidoreductase [Acidiphilium].
ACCESSION WP_035229192
VERSION WP_035229192.1
KEYWORDS RefSeq.
SOURCE Acidiphilium
ORGANISM Acidiphilium
Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
Acetobacteraceae.
REFERENCE 1 (residues 1 to 522)
AUTHORS Wongnate,T. and Chaiyen,P.
TITLE The substrate oxidation mechanism of pyranose 2-oxidase and other
related enzymes in the glucose-methanol-choline superfamily
JOURNAL FEBS J 280 (13), 3009-3027 (2013)
PUBMED 23578136
REFERENCE 2 (residues 1 to 522)
AUTHORS Sampson,N.S.
TITLE Dissection of a flavoenzyme active site: the reaction catalyzed by
cholesterol oxidase
JOURNAL Antioxid Redox Signal 3 (5), 839-846 (2001)
PUBMED 11761331
COMMENT REFSEQ: This record represents a single, non-redundant, protein
sequence which may be annotated on many different RefSeq genomes
from the same, or different, species.
##Evidence-For-Name-Assignment-START##
Evidence Category :: Conserved Domain (CDD)
Evidence Accession :: Domain architecture ID 11455227
Evidence Source :: NCBI SPARCLE
##Evidence-For-Name-Assignment-END##
COMPLETENESS: full length.
FEATURES Location/Qualifiers
source 1..522
/organism="Acidiphilium"
/db_xref="taxon:522"
Protein 1..522
/product="GMC family oxidoreductase"
/GO_function="GO:0016491 - oxidoreductase activity
[Evidence IEA]"
/calculated_mol_wt=57895
Region 1..522
/region_name="BetA"
/note="Choline dehydrogenase or related flavoprotein
[Lipid transport and metabolism, General function
prediction only]; COG2303"
/db_xref="CDD:225186"
ORIGIN
1 mserydvivi gsgpggasla qrlaptgkri liiergdylp rsqknwdsqt vfvdgayqtk
61 etwhnrkgdk fqpglhyfvg gnskvygaal frlrerdfet ivhkdgispe wpvkydvfep
121 yyaeaerlfh vhgkrgedpn epwssgdfph ppvshearie elsasftrdg lhpfhlplgi
181 llderdgkpt ptstcircda fdgypcllng kadaqvmcid ptlalhpnvt lltnayaetl
241 etdargrsit gvnviragah eryeadivvt acgalssall llrsandahp tglangsdqv
301 grnymrhnqs vlmallrepn dtvfqktlav sdfyfgtddw dyplgliqmc atshadqirg
361 eslpswlsfl pempfetmar hsmdfwlsse dlprsenrit landgrvfld lepnnmeahh
421 rlkkkleaam skagpnlaml drslylgkni plggtahqag tlrfgtdptq svldlnckth
481 eidnlyvtda sffpsigavn ptltiianal rvadhikqri dp
//