ID D0ST13_ACILW Unreviewed; 261 AA.
AC D0ST13;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Putative molybdopterin biosynthesis protein MoeB {ECO:0000313|EMBL:EEY90667.1};
GN ORFNames=HMPREF0017_00437 {ECO:0000313|EMBL:EEY90667.1};
OS Acinetobacter lwoffii SH145.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=575588 {ECO:0000313|EMBL:EEY90667.1, ECO:0000313|Proteomes:UP000018425};
RN [1] {ECO:0000313|Proteomes:UP000018425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH145 {ECO:0000313|Proteomes:UP000018425};
RX PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA Seifert H., Dijkshoorn L.;
RT "The success of Acinetobacter species; genetic, metabolic and virulence
RT attributes.";
RL PLoS ONE 7:E46984-E46984(2012).
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; GG705056; EEY90667.1; -; Genomic_DNA.
DR AlphaFoldDB; D0ST13; -.
DR eggNOG; COG0476; Bacteria.
DR HOGENOM; CLU_013325_10_3_6; -.
DR Proteomes; UP000018425; Unassembled WGS sequence.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR CDD; cd00757; ThiF_MoeB_HesA_family; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953:SF240; SULFUR CARRIER PROTEIN THIS ADENYLYLTRANSFERASE; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 4: Predicted;
FT DOMAIN 23..256
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
SQ SEQUENCE 261 AA; 28821 MW; 8479A1429D2FBE1D CRC64;
MSTFNMDAIS PEFELTDAEL HLYSRQILLD GWDIDAQERL KFSNVCIIGC GGIGCTLAEL
LARAGVGKIT LIDPDTIEMS NLQRQLAFIP QDIGFYKAET LAKRLSQVNP NLQVEYVNQA
LTAENAVSVI EHQDLVLDGC DQFATRYLVN QICVELNMPL LSASAIGLQG QLFMVEGDSA
CYACLFPPEN QADESLRCAD SGVLATTPNV MASLQAHHAL LYLGLGQMPL RQKLLLWDGM
SFKQRILTFE KDTDCPICQA R
//