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Database: UniProt
Entry: K9D6Y3_9FIRM
LinkDB: K9D6Y3_9FIRM
Original site: K9D6Y3_9FIRM 
ID   K9D6Y3_9FIRM            Unreviewed;       264 AA.
AC   K9D6Y3;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Thiamine biosynthesis protein ThiF {ECO:0000313|EMBL:EKU78946.1};
GN   ORFNames=HMPREF9282_00743 {ECO:0000313|EMBL:EKU78946.1};
OS   Veillonella seminalis ACS-216-V-Col6b.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=883156 {ECO:0000313|EMBL:EKU78946.1, ECO:0000313|Proteomes:UP000009891};
RN   [1] {ECO:0000313|EMBL:EKU78946.1, ECO:0000313|Proteomes:UP000009891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-216-V-Col6b {ECO:0000313|EMBL:EKU78946.1,
RC   ECO:0000313|Proteomes:UP000009891};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA   Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Veillonella ratti ACS-216-V-COL6B.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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:EKU78946.1}.
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DR   EMBL; AHAF01000003; EKU78946.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9D6Y3; -.
DR   STRING; 883156.HMPREF9282_00743; -.
DR   PATRIC; fig|883156.3.peg.729; -.
DR   eggNOG; COG0476; Bacteria.
DR   HOGENOM; CLU_013325_10_4_9; -.
DR   OrthoDB; 9804286at2; -.
DR   Proteomes; UP000009891; Unassembled WGS sequence.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR012729; ThiF_fam2.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR032726; ThiS-like_dom.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   NCBIfam; TIGR02354; thiF_fam2; 1.
DR   PANTHER; PTHR43267; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR   PANTHER; PTHR43267:SF1; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   Pfam; PF14453; ThiS-like; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE   4: Predicted;
FT   DOMAIN          1..54
FT                   /note="ThiS-like ubiquitin"
FT                   /evidence="ECO:0000259|Pfam:PF14453"
FT   DOMAIN          70..262
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   264 AA;  28955 MW;  E8F46CF607887BBB CRC64;
     MNITINGQTV SVAPDTVTAD VITNKSDDLW LLNGFAVDSD TPLQDGDALL CVSRNKVPDE
     ATYDAVWNAR YGTEIYTRFK QSHIPVCGAG GLGSHIAISL ARLGIGELTI IDKDVVDLTN
     LGRQAYEMTD LGKPKVYALK NILHRINPFI KVNAVHTTIH SGNYDNYLKD FPYIVEAFDS
     AENKAELTSY VLTHYPQTII IGASGVSGYD HPNTVQTKEL FSRYYQTGDG HSESTIGLLA
     PRVMLCAAHE ATILLHLLLT QKES
//
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