(data stored in ACNUC7421 zone)

SWISSPROT: C6WGN3_ACTMD

ID   C6WGN3_ACTMD            Unreviewed;       237 AA.
AC   C6WGN3;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 45.
DE   RecName: Full=FAD:protein FMN transferase {ECO:0000256|RuleBase:RU363002};
DE            EC=2.7.1.180 {ECO:0000256|RuleBase:RU363002};
GN   OrderedLocusNames=Amir_0382 {ECO:0000313|EMBL:ACU34349.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34349.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34349.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
CC   -!- FUNCTION: Flavin transferase that catalyzes the transfer of the
CC       FMN moiety of FAD and its covalent binding to the hydroxyl group
CC       of a threonine residue in a target flavoprotein.
CC       {ECO:0000256|RuleBase:RU363002}.
CC   -!- CATALYTIC ACTIVITY: FAD + [protein]-L-threonine = [protein]-FMN-L-
CC       threonine + AMP. {ECO:0000256|RuleBase:RU363002}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU363002};
CC   -!- SIMILARITY: Belongs to the ApbE family.
CC       {ECO:0000256|RuleBase:RU363002}.
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DR   EMBL; CP001630; ACU34349.1; -; Genomic_DNA.
DR   RefSeq; WP_012783012.1; NC_013093.1.
DR   ProteinModelPortal; C6WGN3; -.
DR   STRING; 446462.Amir_0382; -.
DR   EnsemblBacteria; ACU34349; ACU34349; Amir_0382.
DR   KEGG; ami:Amir_0382; -.
DR   eggNOG; ENOG4108108; Bacteria.
DR   eggNOG; COG1477; LUCA.
DR   HOGENOM; HOG000252467; -.
DR   KO; K03734; -.
DR   OMA; YERGDHI; -.
DR   OrthoDB; POG091H022B; -.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0017013; P:protein flavinylation; IEA:InterPro.
DR   InterPro; IPR024932; ApbE.
DR   InterPro; IPR003374; ApbE-like.
DR   PANTHER; PTHR30040; PTHR30040; 1.
DR   Pfam; PF02424; ApbE; 2.
DR   SUPFAM; SSF143631; SSF143631; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6WGN3.
DR   SWISS-2DPAGE; C6WGN3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   FAD {ECO:0000256|RuleBase:RU363002};
KW   Flavoprotein {ECO:0000256|RuleBase:RU363002};
KW   Lipoprotein {ECO:0000313|EMBL:ACU34349.1};
KW   Magnesium {ECO:0000256|RuleBase:RU363002};
KW   Metal-binding {ECO:0000256|RuleBase:RU363002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   Transferase {ECO:0000256|RuleBase:RU363002}.
SQ   SEQUENCE   237 AA;  25089 MW;  69E4F59A3E32A46C CRC64;
     MRHVEQVMGF PVSVNVPDGD GHGAAVADVF EWLHEVDARF SPFKPGSEVS RLGRGEDVEP
     SPDLAHVLAV SEWYREATGG AFAVRRGGVL DPCAVVKGWA VERAADLLRS AGVPRFVLNA
     GGDVATEGGP WRVGVRHPDH PDRFCAVLEV DGLAVATSAR YERGDHIVDA RTGEPVTSLL
     SLTVVARSLE VADATATAAF ALGREGVAWA ASRPGCEVHA VDADRRVHRT PGLPLAP
//

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