Entry
Name
sulfur carrier protein ThiS adenylyltransferase;
thiF (gene name)
Class
Transferases;
Transferring phosphorus-containing groups;
Nucleotidyltransferases
BRITE hierarchy
Sysname
ATP:[ThiS] adenylyltransferase
Reaction(IUBMB)
ATP + [ThiS] = diphosphate + adenylyl-[ThiS] [RN:
R07459 ]
Reaction(KEGG)
Substrate
Product
diphosphate [CPD:
C00013 ];
adenylyl-[ThiS]
Comment
Binds Zn2+. The enzyme catalyses the adenylation of ThiS, a sulfur carrier protein involved in the biosynthesis of thiamine.
The enzyme shows significant structural similarity to ubiquitin-activating enzyme [3,4]. In Escherichia coli, but not in Bacillus subtilis, the enzyme forms a cross link from Cys-184 to the ThiS carboxy terminus (the position that is also thiolated) via an acyldisulfide [2].
History
EC 2.7.7.73 created 2011
Pathway
Orthology
K03148 sulfur carrier protein ThiS adenylyltransferase
Genes
ECOO : ECRM13514_5113(thiF)
ECOH : ECRM13516_4849(thiF)
ECW : EcE24377A_4534(thiF)
EDJ : ECDH1ME8569_3852(thiF)
ECOI : ECOPMV1_02797(thiF)
REE : electrica_04813(thiF_2)
RTG : NCTC13098_06934(thiF_2)
CLAP : NCTC11466_04347(thiF_2)
KIE : NCTC12125_03512(thiF_1)
PSHI : SAMEA2665130_3035(thiF)
YPG : YpAngola_A0453(thiF)
YPI : YpsIP31758_3855(thiF)
SMW : SMWW4_v1c02880(thiF)
SFJ : SAMEA4384070_0271(thiF)
SOF : NCTC11214_02089(thiF)
PAQU : DMB82_0001035(moeB)
EHD : ERCIPSTX3056_680(thiF)
TPTY : NCTC11468_00196(thiF)
PHEI : NCTC12003_00402(thiF)
PRJ : NCTC6933_00458(thiF)
LRI : NCTC12151_00409(thiF)
ALIG : NCTC10568_01008(thiF)
VAU : VANGNB10_cI2687c(thiF)
VPL : SA104470976_02678(thiF)
SALH : HMF8227_02268(thiF)
AEL : NCTC12917_00354(thiF)
CJV : MTVDSCj20_1048(thiF)
CFV : CFVI03293_0074(thiF)
CAMP : CFT03427_0079(thiF)
CCOC : CCON33237_0911(thiF)
CLR : UPTC16701_1122(thiF)
CLM : UPTC16712_1153(thiF)
CAMR : CAQ16704_1141(thiF)
CHV : CHELV3228_1280(thiF)
CPIN : CPIN18020_0736(thiF)
CAMZ : CVIC12175_0608(thiF)
CUX : CUP3940_0613(thiFIII)
CNV : CNZW441b_1030(thiFIII)
APOC : APORC_0154(thiFIII)
PCA : Pcar_0611(thiF-2) Pcar_2513(thiF-1)
PACE : A6070_02710 A6070_12660
PSYF : N1030_02265(thiF) N1030_02910
DSB : LN040_00200(thiF) LN040_00895
PPOR : JCM14722_04540 JCM14722_06390
PTHE : LF599_10675 LF599_11515(thiF)
PBIZ : LWC08_12450 LWC08_13535(thiF)
CLIH : KPS_000988(thiF) KPS_002197
DEK : DSLASN_00570 DSLASN_17020
BAZ : BAMTA208_11750(thiF)
BFD : NCTC4823_00323(thiF_1) NCTC4823_00383(thiF_2)
BBAD : K7T73_07485 K7T73_08895
BACL : BS34A_12930(thiF_1)
BACA : FAY30_13895 FAY30_25270
BAQU : K6959_06415 K6959_15480
BASB : M662_01620 M662_11235
NIL : L8T27_002495 L8T27_018465
BGI : BGM20_00075 BGM20_21155
BON : A361_02680 A361_26315
CGOT : J1899_01415 J1899_02375 J1899_21250
CFIR : NAF01_02720 NAF01_24175
CSPG : LS684_02765 LS684_19625 LS684_22800
AAYD : B379_03940 B379_12820
HSAN : MUN89_00240 MUN89_12780
LEX : Len3610_07480 Len3610_08965
BSJ : UP17_10615 UP17_24460
BMUR : ABE28_010685 ABE28_023145
PBUT : DTO10_11050 DTO10_24130
PFRI : L8956_11445 L8956_25930
PERI : RE409_12390 RE409_26940
NMK : CHR53_16575 CHR53_27340
NTM : BTDUT50_04350 BTDUT50_10955
NDT : L1999_10440 L1999_28800
NCM : QNK12_12910 QNK12_30550
NNV : QNH39_07770 QNH39_27295
BLEN : NCTC4824_01717(thiF)
ROD : P8596_12710 P8596_18980
SLMS : MM221_17330 MM221_18010
MJO : FOF60_21040 FOF60_23625
ALKL : MM271_09030 MM271_13030
ALKG : MOJ78_02975 MOJ78_16025
PUK : PU629_02910 PU629_11725
SDP : NCTC12225_02297(moeB_2)
SCAP : AYP1020_1668(moeB_2)
SPIC : SAMEA4384060_0468(moeB_1)
BCOP : JD108_15870 JD108_16400
PCEL : HUB94_08575 HUB94_20590
PPOG : QPK24_06185 QPK24_15470
PLZH : C0638_15455 C0638_16015 C0638_19500
SURL : BI350_02455 BI350_16325
ACG : AWM71_00515 AWM71_06635
CACE : CACET_c37750(thiF2)
CGEL : psyc5s11_15130(moeB)
BPRO : PMF13cell1_01241(tcdA_1)
BLUI : Blut17040_26440(thiF)
CSCI : HDCHBGLK_02706(moeB)
CHYL : CE91St63_07310(moeB)
ETM : CE91St48_39550(moeB)
PDF : CD630DERM_17030(thiF)
PIV : NCTC13079_01345(moeZ_2)
PFAC : PFJ30894_00304(tcdA_1)
SXT : KPP03845_100519(ttuC)
GVA : HMPREF0424_0777(thiF)
CCOS : Pan44_22540(moeB_1)
ALUS : STSP2_02472(moeB_1)
FPOL : ERS445057_00300(moeB_1)
» show all
Taxonomy
Reference
Authors
Taylor SV, Kelleher NL, Kinsland C, Chiu HJ, Costello CA, Backstrom AD, McLafferty FW, Begley TP
Title
Thiamin biosynthesis in Escherichia coli. Identification of ThiS thiocarboxylate as the immediate sulfur donor in the thiazole formation.
Journal
Sequence
Reference
Authors
Xi J, Ge Y, Kinsland C, McLafferty FW, Begley TP
Title
Biosynthesis of the thiazole moiety of thiamin in Escherichia coli: identification of an acyldisulfide-linked protein--protein conjugate that is functionally analogous to the ubiquitin/E1 complex.
Journal
Sequence
Reference
Authors
Duda DM, Walden H, Sfondouris J, Schulman BA
Title
Structural analysis of Escherichia coli ThiF.
Journal
Sequence
Reference
Authors
Lehmann C, Begley TP, Ealick SE.
Title
Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis.
Journal
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.7.7.73
ExPASy - ENZYME nomenclature database: 2.7.7.73
LinkDB
All DBs