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GTP 3',8-cyclase (EC 4.1.99.22) (Molybdenum cofactor biosynthesis protein A)

 MOAA_STAA8              Reviewed;         340 AA.
P69848; Q2FVY5;
24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
10-OCT-2018, entry version 90.
RecName: Full=GTP 3',8-cyclase {ECO:0000303|PubMed:25697423};
EC=4.1.99.22 {ECO:0000269|PubMed:23627491};
AltName: Full=Molybdenum cofactor biosynthesis protein A;
Name=moaA; OrderedLocusNames=SAOUHSC_02536;
Staphylococcus aureus (strain NCTC 8325).
Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
Staphylococcus.
NCBI_TaxID=93061;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NCTC 8325;
Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W.,
Iandolo J.J.;
"The Staphylococcus aureus NCTC 8325 genome.";
(In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
Gram positive pathogens, 2nd edition, pp.381-412, ASM Press,
Washington D.C. (2006).
[2]
EPR SPECTROSCOPY, AND SUBSTRATE BINDING.
PubMed=19566093; DOI=10.1021/ja903978u;
Lees N.S., Haenzelmann P., Hernandez H.L., Subramanian S.,
Schindelin H., Johnson M.K., Hoffman B.M.;
"ENDOR spectroscopy shows that guanine N1 binds to [4Fe-4S] cluster II
of the S-adenosylmethionine-dependent enzyme MoaA: mechanistic
implications.";
J. Am. Chem. Soc. 131:9184-9185(2009).
[3]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
MUTAGENESIS OF ASP-198; 330-ARG--LYS-332; GLY-339 AND GLY-340, AND
REACTION MECHANISM.
PubMed=23627491; DOI=10.1021/ja401781t;
Hover B.M., Loksztejn A., Ribeiro A.A., Yokoyama K.;
"Identification of a cyclic nucleotide as a cryptic intermediate in
molybdenum cofactor biosynthesis.";
J. Am. Chem. Soc. 135:7019-7032(2013).
[4]
FUNCTION OF C-TERMINUS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, AND REACTION MECHANISM.
PubMed=25697423; DOI=10.1021/ja512997j;
Hover B.M., Yokoyama K.;
"C-Terminal glycine-gated radical initiation by GTP 3',8-cyclase in
the molybdenum cofactor biosynthesis.";
J. Am. Chem. Soc. 137:3352-3359(2015).
[5]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF APOPROTEIN AND OF COMPLEX
WITH 4FE-4S AND S-ADENOSYL-L-METHIONINE, SUBUNIT, AND COFACTOR.
STRAIN=ATCC 35556 / SA113;
PubMed=15317939; DOI=10.1073/pnas.0404624101;
Haenzelmann P., Schindelin H.;
"Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA
and its implications for molybdenum cofactor deficiency in humans.";
Proc. Natl. Acad. Sci. U.S.A. 101:12870-12875(2004).
[6]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF WILD-TYPE AND MUTANT
ALA-17/ALA-266/ALA-268 IN COMPLEX WITH 5'-GTP; 4FE-4S AND
S-ADENOSYL-L-METHIONINE, AND MUTAGENESIS OF ARG-17; CYS-24; CYS-28;
TYR-30; CYS-31; LYS-69; ARG-71; THR-73; SER-126; ARG-192; PHE-260;
ARG-266 AND ARG-268.
STRAIN=ATCC 35556 / SA113;
PubMed=16632608; DOI=10.1073/pnas.0510711103;
Haenzelmann P., Schindelin H.;
"Binding of 5'-GTP to the C-terminal FeS cluster of the radical S-
adenosylmethionine enzyme MoaA provides insights into its mechanism.";
Proc. Natl. Acad. Sci. U.S.A. 103:6829-6834(2006).
-!- FUNCTION: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-
dihydroguanosine 5'-triphosphate. {ECO:0000269|PubMed:23627491,
ECO:0000269|PubMed:25697423}.
-!- CATALYTIC ACTIVITY: GTP + S-adenosyl-L-methionine + reduced
electron acceptor = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-
triphosphate + 5'-deoxyadenosine + L-methionine + oxidized
electron acceptor. {ECO:0000269|PubMed:23627491,
ECO:0000269|PubMed:25697423}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000269|PubMed:15317939};
Note=Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster
coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and
the GTP-derived substrate. {ECO:0000269|PubMed:15317939};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.4 uM for GTP {ECO:0000269|PubMed:23627491};
KM=3.1 uM for GTP {ECO:0000269|PubMed:25697423};
KM=4.1 uM for S-adenosyl-L-methionine
{ECO:0000269|PubMed:23627491};
KM=5.1 uM for S-adenosyl-L-methionine
{ECO:0000269|PubMed:25697423};
Note=kcat is 0.045 min(-1). {ECO:0000269|PubMed:23627491,
ECO:0000269|PubMed:25697423};
-!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
{ECO:0000255|HAMAP-Rule:MF_01225}.
-!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:15317939,
ECO:0000269|PubMed:16632608}.
-!- DOMAIN: The central core of the structure is composed of a partial
TIM-barrel fold deviating from the canonical TIM-barrel topology.
-!- SIMILARITY: Belongs to the radical SAM superfamily. MoaA family.
{ECO:0000255|HAMAP-Rule:MF_01225}.
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EMBL; CP000253; ABD31551.1; -; Genomic_DNA.
RefSeq; WP_000230173.1; NZ_LS483365.1.
RefSeq; YP_501000.1; NC_007795.1.
PDB; 1TV7; X-ray; 2.80 A; A/B=1-340.
PDB; 1TV8; X-ray; 2.20 A; A/B=1-340.
PDB; 2FB2; X-ray; 2.25 A; A/B=1-340.
PDB; 2FB3; X-ray; 2.35 A; A/B=1-340.
PDBsum; 1TV7; -.
PDBsum; 1TV8; -.
PDBsum; 2FB2; -.
PDBsum; 2FB3; -.
ProteinModelPortal; P69848; -.
SMR; P69848; -.
STRING; 93061.SAOUHSC_02536; -.
EnsemblBacteria; ABD31551; ABD31551; SAOUHSC_02536.
GeneID; 3921126; -.
KEGG; sao:SAOUHSC_02536; -.
PATRIC; fig|93061.5.peg.2287; -.
eggNOG; ENOG4105CM1; Bacteria.
eggNOG; COG2896; LUCA.
HOGENOM; HOG000228681; -.
KO; K03639; -.
OMA; IEFMPIG; -.
BioCyc; SAUR93061:G1G5Y-2397-MONOMER; -.
UniPathway; UPA00344; -.
EvolutionaryTrace; P69848; -.
PRO; PR:P69848; -.
Proteomes; UP000008816; Chromosome.
GO; GO:0019008; C:molybdopterin synthase complex; IEA:InterPro.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
GO; GO:0061798; F:GTP 3',8'-cyclase activity; IEA:UniProtKB-UniRule.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-UniRule.
GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_01225_B; MoaA_B; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR006638; Elp3/MiaB/NifB.
InterPro; IPR034481; Main_SPASM_domain-containing.
InterPro; IPR013483; MoaA.
InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
InterPro; IPR010505; Mob_synth_C.
InterPro; IPR007197; rSAM.
InterPro; IPR034395; SPASM/twitch_domain-containing.
Pfam; PF06463; Mob_synth_C; 1.
Pfam; PF04055; Radical_SAM; 1.
SFLD; SFLDG01067; SPASM/twitch_domain_containing; 1.
SFLD; SFLDG01383; cyclic_pyranopterin_phosphate_; 1.
SFLD; SFLDG01386; main_SPASM_domain-containing; 1.
SFLD; SFLDS00029; Radical_SAM; 1.
SMART; SM00729; Elp3; 1.
TIGRFAMs; TIGR02666; moaA; 1.
PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
1: Evidence at protein level;
3D-structure; 4Fe-4S; Complete proteome; GTP-binding; Iron;
Iron-sulfur; Lyase; Metal-binding; Molybdenum cofactor biosynthesis;
Nucleotide-binding; Reference proteome; S-adenosyl-L-methionine.
CHAIN 1 340 GTP 3',8-cyclase.
/FTId=PRO_0000152995.
NP_BIND 266 268 GTP. {ECO:0000244|PDB:2FB3,
ECO:0000269|PubMed:16632608}.
METAL 24 24 Iron-sulfur 1 (4Fe-4S-S-AdoMet).
{ECO:0000244|PDB:2FB3,
ECO:0000269|PubMed:16632608}.
METAL 28 28 Iron-sulfur 1 (4Fe-4S-S-AdoMet).
{ECO:0000244|PDB:2FB3,
ECO:0000269|PubMed:16632608}.
METAL 31 31 Iron-sulfur 1 (4Fe-4S-S-AdoMet).
{ECO:0000244|PDB:2FB3,
ECO:0000269|PubMed:16632608}.
METAL 261 261 Iron-sulfur 2 (4Fe-4S-substrate).
{ECO:0000244|PDB:2FB3,
ECO:0000269|PubMed:16632608}.
METAL 264 264 Iron-sulfur 2 (4Fe-4S-substrate).
{ECO:0000244|PDB:2FB3,
ECO:0000269|PubMed:16632608}.
METAL 278 278 Iron-sulfur 2 (4Fe-4S-substrate).
{ECO:0000244|PDB:2FB3,
ECO:0000269|PubMed:16632608}.
BINDING 17 17 GTP. {ECO:0000244|PDB:2FB3,
ECO:0000269|PubMed:16632608}.
BINDING 30 30 S-adenosyl-L-methionine.
{ECO:0000244|PDB:2FB3,
ECO:0000269|PubMed:16632608}.
BINDING 71 71 GTP. {ECO:0000244|PDB:2FB3,
ECO:0000269|PubMed:16632608}.
BINDING 75 75 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000244|PDB:2FB3,
ECO:0000269|PubMed:16632608}.
BINDING 102 102 GTP. {ECO:0000244|PDB:2FB3,
ECO:0000269|PubMed:16632608}.
BINDING 126 126 S-adenosyl-L-methionine.
{ECO:0000244|PDB:2FB3,
ECO:0000269|PubMed:16632608}.
BINDING 163 163 GTP. {ECO:0000244|PDB:2FB3,
ECO:0000269|PubMed:16632608}.
BINDING 197 197 S-adenosyl-L-methionine; via amide
nitrogen and carbonyl oxygen.
{ECO:0000244|PDB:2FB3,
ECO:0000269|PubMed:16632608}.
MUTAGEN 17 17 R->A: Loss of activity.
{ECO:0000269|PubMed:16632608}.
MUTAGEN 24 24 C->A: Loss of activity; when associated
with A-28 and A-31.
{ECO:0000269|PubMed:16632608}.
MUTAGEN 28 28 C->A: Loss of activity; when associated
with A-24 and A-31.
{ECO:0000269|PubMed:16632608}.
MUTAGEN 30 30 Y->A: Reduces activity by over 80%.
{ECO:0000269|PubMed:16632608}.
MUTAGEN 31 31 C->A: Loss of activity; when associated
with A-24 and A-28.
{ECO:0000269|PubMed:16632608}.
MUTAGEN 69 69 K->A: Reduces activity by about 60%.
{ECO:0000269|PubMed:16632608}.
MUTAGEN 71 71 R->A: Strongly reduced affinity for GTP.
Reduces activity by about 80%.
{ECO:0000269|PubMed:16632608}.
MUTAGEN 73 73 T->A: Reduces activity by over 80%.
{ECO:0000269|PubMed:16632608}.
MUTAGEN 126 126 S->A: Reduces activity by over 80%.
{ECO:0000269|PubMed:16632608}.
MUTAGEN 192 192 R->A: Reduces activity by about 80%.
{ECO:0000269|PubMed:16632608}.
MUTAGEN 198 198 D->A: Loss of activity by 92%.
{ECO:0000269|PubMed:25697423}.
MUTAGEN 260 260 F->A: Alters stability of FeS cluster and
alters protein stability.
{ECO:0000269|PubMed:16632608}.
MUTAGEN 260 260 F->L: Reduces activity by about 80%.
{ECO:0000269|PubMed:16632608}.
MUTAGEN 266 266 R->A: Loss of activity. Strongly reduced
affinity for GTP.
{ECO:0000269|PubMed:16632608}.
MUTAGEN 268 268 R->A: Loss of activity.
{ECO:0000269|PubMed:16632608}.
MUTAGEN 330 332 RKK->AAA: Loss of activity by 92%.
{ECO:0000269|PubMed:25697423}.
MUTAGEN 339 339 G->A,S,V: Loss of activity.
{ECO:0000269|PubMed:25697423}.
MUTAGEN 340 340 G->A,S,V: Loss of activity.
{ECO:0000269|PubMed:25697423}.
STRAND 15 19 {ECO:0000244|PDB:2FB2}.
TURN 29 31 {ECO:0000244|PDB:2FB2}.
TURN 34 36 {ECO:0000244|PDB:2FB2}.
HELIX 46 48 {ECO:0000244|PDB:2FB2}.
HELIX 52 64 {ECO:0000244|PDB:2FB2}.
STRAND 69 75 {ECO:0000244|PDB:2FB2}.
HELIX 77 79 {ECO:0000244|PDB:2FB2}.
HELIX 83 90 {ECO:0000244|PDB:2FB2}.
STRAND 98 103 {ECO:0000244|PDB:2FB2}.
HELIX 108 117 {ECO:0000244|PDB:2FB2}.
STRAND 122 126 {ECO:0000244|PDB:2FB2}.
HELIX 132 139 {ECO:0000244|PDB:2FB2}.
HELIX 145 158 {ECO:0000244|PDB:2FB2}.
STRAND 161 169 {ECO:0000244|PDB:2FB2}.
TURN 170 172 {ECO:0000244|PDB:2FB2}.
HELIX 174 176 {ECO:0000244|PDB:2FB2}.
HELIX 177 187 {ECO:0000244|PDB:2FB2}.
STRAND 191 195 {ECO:0000244|PDB:2FB2}.
STRAND 201 205 {ECO:0000244|PDB:2FB2}.
HELIX 213 223 {ECO:0000244|PDB:2FB2}.
STRAND 226 228 {ECO:0000244|PDB:2FB2}.
STRAND 238 243 {ECO:0000244|PDB:2FB2}.
TURN 244 246 {ECO:0000244|PDB:2FB2}.
STRAND 249 253 {ECO:0000244|PDB:2FB2}.
TURN 255 258 {ECO:0000244|PDB:2FB2}.
HELIX 261 263 {ECO:0000244|PDB:2FB2}.
STRAND 266 269 {ECO:0000244|PDB:2FB2}.
STRAND 275 279 {ECO:0000244|PDB:2FB2}.
HELIX 288 293 {ECO:0000244|PDB:2FB2}.
HELIX 298 310 {ECO:0000244|PDB:2FB2}.
HELIX 316 327 {ECO:0000244|PDB:2FB2}.
SEQUENCE 340 AA; 39078 MW; BDCDFE1014E98306 CRC64;
MVEQIKDKLG RPIRDLRLSV TDRCNFRCDY CMPKEVFGDD FVFLPKNELL TFDEMARIAK
VYAELGVKKI RITGGEPLMR RDLDVLIAKL NQIDGIEDIG LTTNGLLLKK HGQKLYDAGL
RRINVSLDAI DDTLFQSINN RNIKATTILE QIDYATSIGL NVKVNVVIQK GINDDQIIPM
LEYFKDKHIE IRFIEFMDVG NDNGWDFSKV VTKDEMLTMI EQHFEIDPVE PKYFGEVAKY
YRHKDNGVQF GLITSVSQSF CSTCTRARLS SDGKFYGCLF ATVDGFNVKA FIRSGVTDEE
LKEQFKALWQ IRDDRYSDER TAQTVANRQR KKINMNYIGG


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