ID Q4JVZ6_CORJK Unreviewed; 425 AA.
AC Q4JVZ6;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Dinucleotide-utilizing enzyme involved in thiamine biosynthesis {ECO:0000313|EMBL:CAI37011.1};
GN Name=thiF {ECO:0000313|EMBL:CAI37011.1};
GN OrderedLocusNames=jk0849 {ECO:0000313|EMBL:CAI37011.1};
OS Corynebacterium jeikeium (strain K411).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=306537 {ECO:0000313|EMBL:CAI37011.1, ECO:0000313|Proteomes:UP000000545};
RN [1] {ECO:0000313|EMBL:CAI37011.1, ECO:0000313|Proteomes:UP000000545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K411 {ECO:0000313|EMBL:CAI37011.1,
RC ECO:0000313|Proteomes:UP000000545};
RX PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005;
RA Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A.,
RA Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F.,
RA Rupp O., Schneiker S., Viehoever P., Puehler A.;
RT "Complete genome sequence and analysis of the multiresistant nosocomial
RT pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the
RT human skin flora.";
RL J. Bacteriol. 187:4671-4682(2005).
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DR EMBL; CR931997; CAI37011.1; -; Genomic_DNA.
DR RefSeq; WP_005295706.1; NC_007164.1.
DR AlphaFoldDB; Q4JVZ6; -.
DR STRING; 306537.jk0849; -.
DR GeneID; 3433256; -.
DR KEGG; cjk:jk0849; -.
DR PATRIC; fig|306537.10.peg.860; -.
DR eggNOG; COG0476; Bacteria.
DR HOGENOM; CLU_013325_1_0_11; -.
DR OrthoDB; 9804286at2; -.
DR Proteomes; UP000000545; Chromosome.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR CDD; cd00158; RHOD; 1.
DR CDD; cd00757; ThiF_MoeB_HesA_family; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953:SF102; ADENYLYLTRANSFERASE AND SULFURTRANSFERASE MOCS3; 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.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000545};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 36..269
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 44707 MW; 8AE47DDA9807FE91 CRC64;
MAGSSHTSSP RTAGTDQAFP AGDFVSLPYR EQRRTARHLN LPGFGPTEQQ RLHDARVLVV
GAGGLGCPAM QSLASAGVGT IVLYDDDTVD VTNLHRQILF SAEDVGRAKV DAATDALKRI
QPDIRVEAHR YRLDANNIVE AFQQVDLVID GSDNFDTKFL VADAAEISGT PLVWTTVLRF
AGQISVFNST ASGERGIGLR DLFPEKPSGD SIPDCASAGV LGATTAVMGA LAATEAIKWV
TGVGQPLLGT VVSYDALTAR TQSFRIAPDP SRQPVVALSP NDNAAASITA CAVQPPEASH
TTPDQDPGSH PAKAPGNAAL HELVRTGKAF TVDVREYHET LLAQPSFIGE QGADEHLAMS
ALADPAGTLD VASPAVAEAF ARHEGTEAVV YCASGVRSQH FVEKYRQVAS EYGITLHNLP
GGVRG
//
