ID D2R5V6_PIRSD Unreviewed; 370 AA.
AC D2R5V6;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Glycine oxidase ThiO {ECO:0000313|EMBL:ADB19041.1};
GN OrderedLocusNames=Psta_4394 {ECO:0000313|EMBL:ADB19041.1};
OS Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella
OS staleyi).
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Pirellula.
OX NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB19041.1, ECO:0000313|Proteomes:UP000001887};
RN [1] {ECO:0000313|EMBL:ADB19041.1, ECO:0000313|Proteomes:UP000001887}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128
RC {ECO:0000313|Proteomes:UP000001887};
RX PubMed=21304671; DOI=10.4056/sigs.51657;
RA Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., Lucas S.,
RA Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Complete genome sequence of Pirellula staleyi type strain (ATCC 27377).";
RL Stand. Genomic Sci. 1:308-316(2009).
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004948}.
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; CP001848; ADB19041.1; -; Genomic_DNA.
DR RefSeq; WP_012913300.1; NC_013720.1.
DR AlphaFoldDB; D2R5V6; -.
DR STRING; 530564.Psta_4394; -.
DR KEGG; psl:Psta_4394; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_4_5_0; -.
DR OrthoDB; 9794226at2; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000001887; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012727; Gly_oxidase_ThiO.
DR NCBIfam; TIGR02352; thiamin_ThiO; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR13847:SF293; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN MNMC; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001887}.
FT DOMAIN 3..353
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 370 AA; 40120 MW; 755A90355866FAB9 CRC64;
MNDCLVIGGG VIGLSIAWEL ARRGQSVQLV DQGKLAREAS WAGAGILPPA ARPLAIHPYD
QLRAMAFEMH REWSARLLRE TGIHNGYQQN GAIYLARSAG EVASLVAWSQ LASDEQVQIE
KLTPARLREI EPAIAPAPSS KPLRATYFLP EECQIRNPRH LQSLIRACQQ AGVELIENSP
LVDLQLHGGE VVAAITSQGE LRAKNYCIAT GAWSGILLQK LGFEVGVLPI RGQMLLLKTD
APILRTIVNE GPRYMVPRDD GHLLIGATEE EVGFDKRNTE EALADLHQFA IELVPSLASA
QVVQSWAGLR PASYDGFPYL GKLPNLANAF VAAGHFRSGL YLSPATAMVM SDLISGITPA
VDLSPFCVLR
//
