ID A2CDJ9_PROM3 Unreviewed; 371 AA.
AC A2CDJ9;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Putative thiamine biosynthesis oxidoreductase {ECO:0000313|EMBL:ABM79559.1};
DE EC=1.4.3.19 {ECO:0000313|EMBL:ABM79559.1};
DE EC=1.4.99.1 {ECO:0000313|EMBL:ABM79559.1};
GN Name=dadA {ECO:0000313|EMBL:ABM79559.1};
GN OrderedLocusNames=P9303_28291 {ECO:0000313|EMBL:ABM79559.1};
OS Prochlorococcus marinus (strain MIT 9303).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=59922 {ECO:0000313|EMBL:ABM79559.1, ECO:0000313|Proteomes:UP000002274};
RN [1] {ECO:0000313|EMBL:ABM79559.1, ECO:0000313|Proteomes:UP000002274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9303 {ECO:0000313|EMBL:ABM79559.1,
RC ECO:0000313|Proteomes:UP000002274};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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DR EMBL; CP000554; ABM79559.1; -; Genomic_DNA.
DR AlphaFoldDB; A2CDJ9; -.
DR STRING; 59922.P9303_28291; -.
DR KEGG; pmf:P9303_28291; -.
DR HOGENOM; CLU_007884_4_5_3; -.
DR BioCyc; PMAR59922:G1G80-2484-MONOMER; -.
DR Proteomes; UP000002274; Chromosome.
DR GO; GO:0043799; F:glycine oxidase activity; IEA:UniProtKB-EC.
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 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 Oxidoreductase {ECO:0000313|EMBL:ABM79559.1}.
FT DOMAIN 9..342
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 371 AA; 40363 MW; 126A36B623D20414 CRC64;
MAAMRTESVL ILGGGLMGLA LAHKLARRGS TVEVLSRRRN EAAGFVAAGM LAPHAEGLSG
EQLRLGQLSL DLIPAWVNQI ETDSGLCCGL RQCGIVVPFA TATQRDLYPT AYLGETLDRS
GLEREVPGLG PNWQAGLLFS QDGQIDNRRR LMRALETACV SLGVRFQEGV EVQEILRDGD
TFRGVRMRNA EGEMHTLTSQ KAVLCCGAWS AQLLPALAIV PVKGQMLSLQ GPRDSLKRIV
FGPGTYLVPR EDGLLVVGAT SEPEAGFMEG LTPFGQQQLQ AGIDTLLPEA SQWPPMERWW
GFRPCTPDGG PLLGRSSVDG LWLATGHHRN GVLLAAITAK LLDKCLGNQP LNKTEQPLMH
AFRWDRFHEQ D
//
