(data stored in ACNUC7421 zone)

SWISSPROT: MOAA_SHEDO

ID   MOAA_SHEDO              Reviewed;         337 AA.
AC   Q12T28;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 88.
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};
GN   OrderedLocusNames=Sden_0101;
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-
CC       dihydroguanosine 5'-triphosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_01225}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-
CC         7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A +
CC         H(+) + L-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
CC       coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
CC       methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and
CC       the GTP-derived 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; CP000302; ABE53398.1; -; Genomic_DNA.
DR   SMR; Q12T28; -.
DR   STRING; 318161.Sden_0101; -.
DR   PRIDE; Q12T28; -.
DR   EnsemblBacteria; ABE53398; ABE53398; Sden_0101.
DR   KEGG; sdn:Sden_0101; -.
DR   eggNOG; ENOG4105CM1; Bacteria.
DR   eggNOG; COG2896; LUCA.
DR   HOGENOM; HOG000228682; -.
DR   KO; K03639; -.
DR   OMA; IEFMPIG; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001982; Chromosome.
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; 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.
PE   3: Inferred from homology;
DR   PRODOM; Q12T28.
DR   SWISS-2DPAGE; Q12T28.
KW   4Fe-4S; Complete proteome; GTP-binding; Iron; Iron-sulfur; Lyase;
KW   Metal-binding; Molybdenum cofactor biosynthesis; Nucleotide-binding;
KW   Reference proteome; S-adenosyl-L-methionine.
FT   CHAIN         1    337       GTP 3',8-cyclase.
FT                                /FTId=PRO_1000085708.
FT   NP_BIND     270    272       GTP. {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   METAL        34     34       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   METAL        38     38       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   METAL        41     41       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   METAL       265    265       Iron-sulfur 2 (4Fe-4S-substrate).
FT                                {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   METAL       268    268       Iron-sulfur 2 (4Fe-4S-substrate).
FT                                {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   METAL       282    282       Iron-sulfur 2 (4Fe-4S-substrate).
FT                                {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   BINDING      27     27       GTP. {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   BINDING      40     40       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   BINDING      76     76       GTP. {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   BINDING      80     80       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01225}.
FT   BINDING     107    107       GTP. {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   BINDING     131    131       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   BINDING     168    168       GTP. {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   BINDING     202    202       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01225}.
SQ   SEQUENCE   337 AA;  37728 MW;  68782B9CEF7BD8BD CRC64;
     MHSPPALGKV NMSQLQDNFG RRFHYLRLSI TDACNFKCTY CLPDGYQSQG NSPFLSLSEI
     ELLLGAFSQM GTQKVRITGG EPSLRKDFID IIGLAANTPN IKTVATTTNG YRLAKNAQAW
     YDAGLRRINV SIDSLDPKMF YQITGENRFD QVMRGVDAAL ESGFERVKIN AVLLKGLNSQ
     DLPRFLHWIK HMPVDLRFIE LMETGLGREY FKAHHLAGTQ VKQQLIRDGW QLDKADILDG
     PAQNFSHSDY QGRIGLIMPY EKNFCVSCNR LRVSAKGQLH LCLFTENGVN LKDLLQDKSQ
     TPELMARLQQ QLGFKTAAHS LHQGITGVTT HLASIGG
//

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