(data stored in ACNUC7421 zone)

SWISSPROT: C6WHY7_ACTMD

ID   C6WHY7_ACTMD            Unreviewed;       341 AA.
AC   C6WHY7;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 67.
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=Amir_0471 {ECO:0000313|EMBL:ACU34438.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34438.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34438.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
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:SAAS00808862}.
CC   -!- CATALYTIC ACTIVITY: GTP + S-adenosyl-L-methionine + reduced
CC       electron acceptor = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-
CC       triphosphate + 5'-deoxyadenosine + L-methionine + oxidized
CC       electron acceptor. {ECO:0000256|HAMAP-Rule:MF_01225,
CC       ECO:0000256|SAAS:SAAS00817830}.
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01225, ECO:0000256|SAAS:SAAS00817832}.
CC   -!- SUBUNIT: Monomer and homodimer. {ECO:0000256|SAAS:SAAS00234447}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. MoaA family.
CC       {ECO:0000256|HAMAP-Rule:MF_01225, ECO:0000256|SAAS:SAAS00808869}.
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DR   EMBL; CP001630; ACU34438.1; -; Genomic_DNA.
DR   ProteinModelPortal; C6WHY7; -.
DR   STRING; 446462.Amir_0471; -.
DR   EnsemblBacteria; ACU34438; ACU34438; Amir_0471.
DR   KEGG; ami:Amir_0471; -.
DR   eggNOG; ENOG4105CM1; Bacteria.
DR   eggNOG; COG2896; LUCA.
DR   HOGENOM; HOG000228681; -.
DR   KO; K03639; -.
DR   OMA; IEFMPIG; -.
DR   OrthoDB; POG091H01YJ; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0019008; C:molybdopterin synthase complex; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0061798; F:GTP 3',8'-cyclase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-HAMAP.
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; IPR034481; Main_SPASM_domain-containing.
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   SFLD; SFLDG01383; cyclic_pyranopterin_phosphate_; 1.
DR   SFLD; SFLDG01386; main_SPASM_domain-containing; 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; C6WHY7.
DR   SWISS-2DPAGE; C6WHY7.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00803661};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00817847};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01225, ECO:0000256|SAAS:SAAS00803669};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00803637};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00817846};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00803678};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00817827};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00817849};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00803656}.
FT   DOMAIN       25    221       Elp3. {ECO:0000259|SMART:SM00729}.
FT   NP_BIND     273    275       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL        35     35       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL        39     39       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL        42     42       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL       268    268       Iron-sulfur 2 (4Fe-4S-substrate).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL       271    271       Iron-sulfur 2 (4Fe-4S-substrate).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL       285    285       Iron-sulfur 2 (4Fe-4S-substrate).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING      28     28       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING      41     41       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING      79     79       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING      83     83       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01225}.
FT   BINDING     110    110       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING     134    134       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING     171    171       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING     205    205       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
SQ   SEQUENCE   341 AA;  36887 MW;  058004AA8D4BBE1C CRC64;
     MRSAPHVTAR PESPSLIDRF GRVATDLRVS LTDKCNLRCT YCMPAEGLDW LRGPELLSDE
     ELVRVIGIAV TRLGVTDVRF TGGEPLLRRG LEDVLAATTA LEPRPRTSMT TNGISLATRA
     AGLKAAGLDR VNVSLDTLDR ERFRELTRRD RLPDVLAGLA AAREAGLEPV KINSVLMRGV
     NDDEAVALVE FAVEHGYQLR FIEQMPLDPQ HGWDRSEMVT AQEILDALGT RFALAPVLAR
     GAAPAERWVV DGGPSVVGVI AAVTRPFCAA CDRTRLTADG QVRNCLFSGA ETDLRALLRS
     GASDEEVAER WRGNAWAKAE GHGIDGDGFA QPDRPMSAIG G
//

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