(data stored in SCRATCH9089 zone)

SWISSPROT: MOAA_PASMU

ID   MOAA_PASMU              Reviewed;         337 AA.
AC   Q9CN21;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 113.
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=PM0625;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02709.1; -; Genomic_DNA.
DR   RefSeq; WP_010906760.1; NC_002663.1.
DR   SMR; Q9CN21; -.
DR   EnsemblBacteria; AAK02709; AAK02709; PM0625.
DR   KEGG; pmu:PM0625; -.
DR   PATRIC; fig|272843.6.peg.633; -.
DR   eggNOG; ENOG4105CM1; Bacteria.
DR   eggNOG; COG2896; LUCA.
DR   HOGENOM; HOG000228682; -.
DR   KO; K03639; -.
DR   OMA; IEFMPIG; -.
DR   BioCyc; PMUL272843:G1FZ8-658-MONOMER; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000809; 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; 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; Q9CN21.
DR   SWISS-2DPAGE; Q9CN21.
KW   4Fe-4S; GTP-binding; Iron; Iron-sulfur; Lyase; Metal-binding;
KW   Molybdenum cofactor biosynthesis; Nucleotide-binding; Reference proteome;
KW   S-adenosyl-L-methionine.
FT   CHAIN           1..337
FT                   /note="GTP 3',8-cyclase"
FT                   /id="PRO_0000152979"
FT   NP_BIND         270..272
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           33
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           37
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           40
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           265
FT                   /note="Iron-sulfur 2 (4Fe-4S-substrate)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           268
FT                   /note="Iron-sulfur 2 (4Fe-4S-substrate)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           282
FT                   /note="Iron-sulfur 2 (4Fe-4S-substrate)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         26
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         39
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         76
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         80
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         107
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         131
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         168
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         202
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen and
FT                   carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
SQ   SEQUENCE   337 AA;  38208 MW;  6F632D29B89588F3 CRC64;
     MQTIPIKHVG NDPLVDAFQR RYYYLRLSIT DVCNFRCNYC LPNGYQPESN KPSFLTLNEI
     RLVVKSFANM GTEKVRITGG EPTLRKDFLP IVETIAQNPT IKQIALTTNG YRMAKDVAAW
     KEAGITSINV SIDSLDARMF HRITGIDKFE DVMRGLERAF EVGYQKIKVN SVLMRDLNDA
     DFNQFLTWIK DKPIQMRFIE LMQTGEMDHF FQQHHVSGQL LADKLINAGW TLQSKGLLDG
     PAKVFKHPDY VGEVGLIMPY EKNFCASCNR LRVSAKGKLH LCLFGEEGIT LRDLLQSDDQ
     QLQLQARISS ALQGKREHHF LHQGDSGVRA NLASIGG
//

If you have problems or comments...

PBIL Back to PBIL home page