ID Q9KVS6_VIBCH Unreviewed; 258 AA.
AC Q9KVS6;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=ThiF protein {ECO:0000313|EMBL:AAF93241.1};
GN OrderedLocusNames=VC_0063 {ECO:0000313|EMBL:AAF93241.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277 {ECO:0000313|EMBL:AAF93241.1, ECO:0000313|Proteomes:UP000000584};
RN [1] {ECO:0000313|EMBL:AAF93241.1, ECO:0000313|Proteomes:UP000000584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961
RC {ECO:0000313|Proteomes:UP000000584};
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D., Ermolaeva M.D.,
RA Vamathevan J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.,
RA Utterback T., Fleishmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR612731-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR612731-3};
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; AE003852; AAF93241.1; -; Genomic_DNA.
DR PIR; B82369; B82369.
DR RefSeq; NP_229722.1; NC_002505.1.
DR RefSeq; WP_000954515.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KVS6; -.
DR STRING; 243277.VC_0063; -.
DR DNASU; 2614106; -.
DR EnsemblBacteria; AAF93241; AAF93241; VC_0063.
DR KEGG; vch:VC_0063; -.
DR PATRIC; fig|243277.26.peg.61; -.
DR eggNOG; COG0476; Bacteria.
DR HOGENOM; CLU_013325_10_3_6; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IBA:GO_Central.
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; IPR012731; Adenyl_ThiF.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR NCBIfam; TIGR02356; adenyl_thiF; 1.
DR PANTHER; PTHR10953:SF194; MOLYBDOPTERIN-SYNTHASE 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;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR612731-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR612731-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR612731-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000584};
KW Zinc {ECO:0000256|PIRSR:PIRSR612731-3}.
FT DOMAIN 10..243
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT ACT_SITE 184
FT /note="Glycyl persulfide ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-1"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-2"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-2"
FT BINDING 60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-2"
FT BINDING 71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-2"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-2"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-2"
FT BINDING 128..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-2"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-3"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-3"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-3"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-3"
FT CROSSLNK 184
FT /note="Glycyl cysteine dithioester (Cys-Gly) (interchain
FT with G-Cter in ThiS)"
FT /evidence="ECO:0000256|PIRSR:PIRSR612731-4"
SQ SEQUENCE 258 AA; 28552 MW; 60CD9B883DE7432B CRC64;
MLTDKQFLRY QRQISLAELG EEGQQKLLNS RVLIVGCGGL GNVVAPYLVG AGVGQVIIAD
SDRLELHNLH RQICYHEAQI GHNKAELLAR YLRELNSEVR VRVIAREVDE LILNLEINQV
DLVLDCSDNL PTRHAINRAC YAAQRPLISG AVIGWEGHLM AFDYRQSTPC YQCVVPDMAE
RQRCSDRGVI GPVVGMIGNG QALIALHALM GSAHFPANQL LRFDGKSMNW QSLQLHPDKV
CPVCSVSSPA QPKEPQPC
//
