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Database: UniProt
Entry: Q97F32_CLOAB
LinkDB: Q97F32_CLOAB
Original site: Q97F32_CLOAB 
ID   Q97F32_CLOAB            Unreviewed;       266 AA.
AC   Q97F32;
DT   01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   SubName: Full=Dinucleotide-utilizing enzyme involved in molybdopterin/thiamine biosynthesis {ECO:0000313|EMBL:AAK80865.1};
GN   OrderedLocusNames=CA_C2923 {ECO:0000313|EMBL:AAK80865.1};
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK80865.1, ECO:0000313|Proteomes:UP000000814};
RN   [1] {ECO:0000313|EMBL:AAK80865.1, ECO:0000313|Proteomes:UP000000814}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC   {ECO:0000313|Proteomes:UP000000814};
RX   PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA   Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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DR   EMBL; AE001437; AAK80865.1; -; Genomic_DNA.
DR   PIR; F97259; F97259.
DR   RefSeq; NP_349525.1; NC_003030.1.
DR   RefSeq; WP_010966206.1; NC_003030.1.
DR   AlphaFoldDB; Q97F32; -.
DR   STRING; 272562.CA_C2923; -.
DR   GeneID; 44999411; -.
DR   KEGG; cac:CA_C2923; -.
DR   PATRIC; fig|272562.8.peg.3107; -.
DR   eggNOG; COG0476; Bacteria.
DR   HOGENOM; CLU_013325_10_4_9; -.
DR   OrthoDB; 9804286at2; -.
DR   Proteomes; UP000000814; Chromosome.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   CDD; cd01487; E1_ThiF_like; 1.
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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000814}.
FT   DOMAIN          1..57
FT                   /note="ThiS-like ubiquitin"
FT                   /evidence="ECO:0000259|Pfam:PF14453"
FT   DOMAIN          75..263
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   266 AA;  29348 MW;  FFBC614BC3BE3FE7 CRC64;
     MKVYVNERSL DVKNGTTLMQ LKRQIKKDSD VVVYNGFIMK KDLSLKEEDN VVFIKKGEIP
     KKEDMEAQLV SRHTPKVHEK VKNTSVGIAG LGGLGSNAAV SLARIGVGRL VLVDFDVVEP
     SNLNRQHYFI RHIGMKKTEA LKEIISQCNP FVKVDVVDTF INGNNAQEIF KDVDIIVEAF
     DNPVCKAELI NSVLTKMNGK KVIGASGMAG YFSSNSIVTK KINKNFYIVG DGENEAAPGC
     GLMAPRVNIA ANHEANQVLR IIMENE
//
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