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Database: UniProt
Entry: A0A1Q7ULF2_9CHLR
LinkDB: A0A1Q7ULF2_9CHLR
Original site: A0A1Q7ULF2_9CHLR 
ID   A0A1Q7ULF2_9CHLR        Unreviewed;       280 AA.
AC   A0A1Q7ULF2;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   28-JUN-2023, entry version 10.
DE   SubName: Full=Myristoyl transferase {ECO:0000313|EMBL:OLE01589.1};
GN   ORFNames=AUG82_10920 {ECO:0000313|EMBL:OLE01589.1};
OS   Ktedonobacter sp. 13_1_20CM_4_53_11.
OC   Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC   Ktedonobacteraceae; Ktedonobacter.
OX   NCBI_TaxID=1805225 {ECO:0000313|EMBL:OLE01589.1, ECO:0000313|Proteomes:UP000186213};
RN   [1] {ECO:0000313|EMBL:OLE01589.1, ECO:0000313|Proteomes:UP000186213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OLE01589.1}.
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DR   EMBL; MNIY01000203; OLE01589.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7ULF2; -.
DR   STRING; 1805225.AUG82_10920; -.
DR   Proteomes; UP000186213; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR027939; NMT1/THI5.
DR   InterPro; IPR015168; SsuA/THI5.
DR   PANTHER; PTHR31528; 4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE PHOSPHATE SYNTHASE THI11-RELATED; 1.
DR   PANTHER; PTHR31528:SF3; THIAMINE BIOSYNTHESIS PROTEIN HI_0357-RELATED; 1.
DR   Pfam; PF09084; NMT1; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE   4: Predicted;
KW   Transferase {ECO:0000313|EMBL:OLE01589.1}.
FT   DOMAIN          3..196
FT                   /note="SsuA/THI5-like"
FT                   /evidence="ECO:0000259|Pfam:PF09084"
SQ   SEQUENCE   280 AA;  30519 MW;  BDF44CC5AE9F96A1 CRC64;
     MLRDEGINLQ LLPYSANVSA DVLVSSGKAD VGISSTEGIV ADAAVNQPVV SIAAIIQHNT
     SALITLANSG ITRPRDLSGK VYGGFGAPYE SAVVGEIIKQ DGGTGQFKNV TLSVDAMQAL
     ESRRIDFVWV FEGWEVIQAQ RAGVKLHIFP ITNYGVADYY TPNIITSPNE IKQKPDLLRR
     FMAATAKGYE YTRTHAQDSA QMLLSANPQG TFPDPGLVVA SQEFLSPRYA DRGRKWGWQD
     AAAWHGYPQF IINSNGIDDA AGHPIHSMDF NRLYTNQFLA
//
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