(data stored in SCRATCH3701 zone)

SWISSPROT: MOAA_ECOBW

ID   MOAA_ECOBW              Reviewed;         329 AA.
AC   C4ZXV3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   11-DEC-2019, entry version 61.
DE   RecName: Full=GTP 3',8-cyclase {ECO:0000255|HAMAP-Rule:MF_01225};
DE            EC=4.1.99.22 {ECO:0000255|HAMAP-Rule:MF_01225};
DE   AltName: Full=Molybdenum cofactor biosynthesis protein A {ECO:0000255|HAMAP-Rule:MF_01225};
GN   Name=moaA {ECO:0000255|HAMAP-Rule:MF_01225}; OrderedLocusNames=BWG_0634;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(2009).
CC   -!- FUNCTION: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-
CC       dihydroguanosine 5'-triphosphate. {ECO:0000255|HAMAP-Rule:MF_01225}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-
CC         dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-
CC         methionine; Xref=Rhea:RHEA:49576, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:131766; EC=4.1.99.22; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01225};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01225};
CC       Note=Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated
CC       with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1
CC       [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived
CC       substrate. {ECO:0000255|HAMAP-Rule:MF_01225};
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01225}.
CC   -!- SUBUNIT: Monomer and homodimer. {ECO:0000255|HAMAP-Rule:MF_01225}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. MoaA family.
CC       {ECO:0000255|HAMAP-Rule:MF_01225}.
DR   EMBL; CP001396; ACR63797.1; -; Genomic_DNA.
DR   RefSeq; WP_001350494.1; NC_012759.1.
DR   SMR; C4ZXV3; -.
DR   EnsemblBacteria; ACR63797; ACR63797; BWG_0634.
DR   KEGG; ebw:BWG_0634; -.
DR   HOGENOM; HOG000228682; -.
DR   KO; K03639; -.
DR   OMA; IEFMPIG; -.
DR   BioCyc; ECOL595496:BWG_RS03595-MONOMER; -.
DR   UniPathway; UPA00344; -.
DR   GO; GO:0019008; C:molybdopterin synthase complex; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061798; F:GTP 3',8'-cyclase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01225_B; MoaA_B; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR013483; MoaA.
DR   InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR   InterPro; IPR010505; Mob_synth_C.
DR   InterPro; IPR007197; rSAM.
DR   Pfam; PF06463; Mob_synth_C; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR02666; moaA; 1.
DR   PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4ZXV3.
DR   SWISS-2DPAGE; C4ZXV3.
KW   4Fe-4S; GTP-binding; Iron; Iron-sulfur; Lyase; Metal-binding;
KW   Molybdenum cofactor biosynthesis; Nucleotide-binding;
KW   S-adenosyl-L-methionine.
FT   CHAIN           1..329
FT                   /note="GTP 3',8-cyclase"
FT                   /id="PRO_1000213997"
FT   NP_BIND         262..264
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           24
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           28
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           31
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           257
FT                   /note="Iron-sulfur 2 (4Fe-4S-substrate)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           260
FT                   /note="Iron-sulfur 2 (4Fe-4S-substrate)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           274
FT                   /note="Iron-sulfur 2 (4Fe-4S-substrate)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         17
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         30
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         68
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         72
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         99
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         123
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         160
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         194
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen and
FT                   carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
SQ   SEQUENCE   329 AA;  37346 MW;  FE91263C53F33F78 CRC64;
     MASQLTDAFA RKFYYLRLSI TDVCNFRCTY CLPDGYKPSG VTNKGFLTVD EIRRVTRAFA
     RLGTEKVRLT GGEPSLRRDF TDIIAAVREN DAIRQIAVTT NGYRLERDVA SWRDAGLTGI
     NVSVDSLDAR QFHAITGQDK FNQVMAGIDA AFEAGFEKVK VNTVLMRDVN HHQLDTFLNW
     IQHRPIQLRF IELMETGEGS ELFRKHHISG QVLRDELLRR GWIHQLRQRS DGPAQVFCHP
     DYAGEIGLIM PYEKDFCATC NRLRVSSIGK LHLCLFGEGG VNLRDLLEDD TQQQALEARI
     SAALREKKQT HFLHQNNTGI TQNLSYIGG
//

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