(data stored in SCRATCH zone)

SWISSPROT: A1SE80_NOCSJ

ID   A1SE80_NOCSJ            Unreviewed;       329 AA.
AC   A1SE80;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   08-MAY-2019, entry version 98.
DE   RecName: Full=GTP 3',8-cyclase {ECO:0000256|HAMAP-Rule:MF_01225};
DE            EC=4.1.99.22 {ECO:0000256|HAMAP-Rule:MF_01225};
DE   AltName: Full=Molybdenum cofactor biosynthesis protein A {ECO:0000256|HAMAP-Rule:MF_01225};
GN   Name=moaA {ECO:0000256|HAMAP-Rule:MF_01225};
GN   OrderedLocusNames=Noca_0574 {ECO:0000313|EMBL:ABL80115.1};
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL80115.1, ECO:0000313|Proteomes:UP000000640};
RN   [1] {ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
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., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Mattes T., Gossett J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABL80115.1, ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RX   PubMed=21551312; DOI=10.1128/JB.05109-11;
RA   Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C.,
RA   Copeland A., Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A.,
RA   Hammon N.M., Han S., Hauser L.J., Israni S., Kim E., Kyrpides N.,
RA   Land M.L., Lapidus A., Larimer F.W., Lucas S., Pitluck S.,
RA   Richardson P., Schmutz J., Tapia R., Thompson S., Tice H.N.,
RA   Spain J.C., Gossett J.G., Mattes T.E.;
RT   "Genome Sequence of the ethene- and vinyl chloride-oxidizing
RT   actinomycete Nocardioides sp. strain JS614.";
RL   J. Bacteriol. 193:3399-3400(2011).
CC   -!- FUNCTION: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-
CC       dihydroguanosine 5'-triphosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_01225, ECO:0000256|SAAS:SAAS01106981}.
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:0000256|HAMAP-
CC         Rule:MF_01225, ECO:0000256|SAAS:SAAS01128401};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_01225};
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01225, ECO:0000256|SAAS:SAAS00138294}.
CC   -!- SUBUNIT: Monomer and homodimer. {ECO:0000256|HAMAP-Rule:MF_01225,
CC       ECO:0000256|SAAS:SAAS00911699}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. MoaA family.
CC       {ECO:0000256|HAMAP-Rule:MF_01225, ECO:0000256|SAAS:SAAS01106980}.
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DR   EMBL; CP000509; ABL80115.1; -; Genomic_DNA.
DR   RefSeq; WP_011754064.1; NC_008699.1.
DR   STRING; 196162.Noca_0574; -.
DR   EnsemblBacteria; ABL80115; ABL80115; Noca_0574.
DR   KEGG; nca:Noca_0574; -.
DR   eggNOG; ENOG4105CM1; Bacteria.
DR   eggNOG; COG2896; LUCA.
DR   HOGENOM; HOG000228680; -.
DR   KO; K03639; -.
DR   OMA; DYLRMSV; -.
DR   OrthoDB; 1199289at2; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000640; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; A1SE80.
DR   SWISS-2DPAGE; A1SE80.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00138299};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000640};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00138126};
KW   Hydrolase {ECO:0000313|EMBL:ABL80115.1};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01225, ECO:0000256|SAAS:SAAS00138256};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00138121};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00138219};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00138296};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00138110};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00138119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000640};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00138251}.
FT   DOMAIN       14    208       Elp3. {ECO:0000259|SMART:SM00729}.
FT   NP_BIND     261    263       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL        24     24       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL        28     28       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL        31     31       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL       256    256       Iron-sulfur 2 (4Fe-4S-substrate).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL       259    259       Iron-sulfur 2 (4Fe-4S-substrate).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL       273    273       Iron-sulfur 2 (4Fe-4S-substrate).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING      17     17       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING      30     30       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING      68     68       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING      72     72       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01225}.
FT   BINDING      97     97       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING     121    121       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING     158    158       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING     192    192       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
SQ   SEQUENCE   329 AA;  35901 MW;  D1CB7752694CA4AD CRC64;
     MTAPLADRFG RVAADLRVSL TDRCNLRCNY CMPAEGLDWL PTEQTLTDDE IVRLITIGVE
     MLGIREVRFT GGEPLLRRGL VDIVARTHAL GVETSLTTNA LGLARTAQAL ADARLDRINA
     SIDTVRPDTF ATITRRDRLH DVVAGLEAAK SAGLGPIKLN AVLLRGTNDD QAPELLRWSI
     EHGYELRFIE QMPLDAQHDW SRAEMVTADE IFDALSTEFS LTPHGEPRGS APAELFDVGG
     GPATVGIIAS VTRPFCGDCD RVRLTADGQV RNCLFAREES DLRTALRSGA TDQEIAERWV
     IAMLGKRAGH GIDDMTFLQP DRPMSAIGG
//

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