ID A0A1M3H759_9SPHI Unreviewed; 469 AA.
AC A0A1M3H759;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Thiamine biosynthesis protein ThiF {ECO:0008006|Google:ProtNLM};
GN ORFNames=BGO55_11740 {ECO:0000313|EMBL:OJW54360.1};
OS Sphingobacteriales bacterium 50-39.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895841 {ECO:0000313|EMBL:OJW54360.1, ECO:0000313|Proteomes:UP000184242};
RN [1] {ECO:0000313|EMBL:OJW54360.1, ECO:0000313|Proteomes:UP000184242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=50-39 {ECO:0000313|EMBL:OJW54360.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJW54360.1}.
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; MKTZ01000025; OJW54360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3H759; -.
DR STRING; 1895841.BGO55_11740; -.
DR Proteomes; UP000184242; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR028090; JAB_dom_prok.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR43267; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR PANTHER; PTHR43267:SF1; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR Pfam; PF14464; Prok-JAB; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 12..117
FT /note="JAB"
FT /evidence="ECO:0000259|Pfam:PF14464"
FT DOMAIN 182..412
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
SQ SEQUENCE 469 AA; 52692 MW; 78E37426EDA55F27 CRC64;
MTYELRFPGK FHEQLRQHLF PGDGLEAVAV VLCGRHEGEG CSILLAHQVV LIPYEECDRT
PDRITWSTKR VLPLLEEVEK RKFALLKIHS HPGGYNRFSH IDDASDDEFF STVYSWSETD
QVHGSAIMLP DGKVFGRIVT HDLQKIPFDT VSMAGDQIRI WRSTNGSSAE ADRDGFSLRN
RQVFGEATHA LVKTLRVGVV GCSGTGSPTI EQLFRLGVGE LVLVDPKPVE DKNLNRIIQS
RKEDVRQRMN KSDMLKAAIE GVELATRVYS YPVSLFDSKE ALLHLIRCDV LFGCVDSAEG
RHLLGLLANF YLIPYFDLGV QLNADGKGGI DSISAVVHYI QPGMSSLLSR NAYSAELLEA
EGLARRSPEE YQERLKVGYI RNTNVERPAV LPVNMLISSM SVIDSLNRLH DTPFKEDSPG
DYARMLMDYA ANCIENRAEK KFPVDELASR FTGRGDYKPF LRMPDLDRL
//
