ID Q47ZL9_COLP3 Unreviewed; 528 AA.
AC Q47ZL9;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:AAZ24920.1};
GN OrderedLocusNames=CPS_3053 {ECO:0000313|EMBL:AAZ24920.1};
OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS psychroerythus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=167879 {ECO:0000313|EMBL:AAZ24920.1, ECO:0000313|Proteomes:UP000000547};
RN [1] {ECO:0000313|EMBL:AAZ24920.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34H {ECO:0000313|EMBL:AAZ24920.1};
RX PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT "The psychrophilic lifestyle as revealed by the genome sequence of
RT Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000083; AAZ24920.1; -; Genomic_DNA.
DR RefSeq; WP_011043840.1; NC_003910.7.
DR AlphaFoldDB; Q47ZL9; -.
DR STRING; 167879.CPS_3053; -.
DR KEGG; cps:CPS_3053; -.
DR HOGENOM; CLU_008878_4_0_6; -.
DR Proteomes; UP000000547; 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; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 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;
FT DOMAIN 89..308
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 396..514
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 528 AA; 57247 MW; D97522747D2C9A6E CRC64;
MTNIAKFDLD DDDLVVIIGS GAGGGTVANE LAQKGVRSVV LEAGKRFTLE DLKNSEWEMF
MKLSWLDKRI SAGGWHHAKN HSGLPAWIVK GVGGSSIHWA GVSLRFKPHE FKMKSTNGVI
EGANVADWPI SYDDIAPYYE KAEDKMGVTG TKATGTPDLP ENSHTKLHRV AAERTGMTFS
NAPMAINSVA RDGRPACQQI GFCMQGCRIG AKWSTMYTEI PKAEATGLCE IRPNSMVLKI
EHDEDGRASG VHYVDENGNK KLQKARIVCV AGNSIESPRL LLNSASKKFP DGLANSSGQV
GRNYMGHVTG GVYGVFPKPV NMHRGTSVPS LITSEQRNDP DRGFVAGYSL EVLSLGLGFL
SAFLKPGTSG WGREVSEALE NYQNMAGVWI CGEDLPVETN RITLHPTEKD QNGLPVPVIT
KTDHNNDLVM RNHAYAQTAK LYKSVGATKL HNLPAYPNSH NMGTNRMSEK ASDGVVNKWG
QSHDVPNLFI SDGSQFVTSA AVNPTLTIVA LAIRQAEHIA KLVKTNAL
//