(data stored in ACNUC9435 zone)

SWISSPROT: MOAA_LISIN

ID   MOAA_LISIN              Reviewed;         333 AA.
AC   Q92CY2;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   11-DEC-2019, entry version 108.
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=lin1039;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(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; AL596167; CAC96270.1; -; Genomic_DNA.
DR   PIR; AF1562; AF1562.
DR   RefSeq; WP_010990725.1; NC_003212.1.
DR   SMR; Q92CY2; -.
DR   STRING; 272626.lin1039; -.
DR   PRIDE; Q92CY2; -.
DR   EnsemblBacteria; CAC96270; CAC96270; CAC96270.
DR   KEGG; lin:lin1039; -.
DR   eggNOG; ENOG4105CM1; Bacteria.
DR   eggNOG; COG2896; LUCA.
DR   HOGENOM; HOG000228680; -.
DR   KO; K03639; -.
DR   OMA; IEFMPIG; -.
DR   OrthoDB; 1199289at2; -.
DR   BioCyc; GCF_000195795:LIN_RS05305-MONOMER; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000002513; 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; Q92CY2.
DR   SWISS-2DPAGE; Q92CY2.
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..333
FT                   /note="GTP 3',8-cyclase"
FT                   /id="PRO_0000152970"
FT   NP_BIND         262..264
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           23
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           27
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           30
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         16
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         29
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         66
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         70
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         97
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         121
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         158
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         192
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen and
FT                   carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
SQ   SEQUENCE   333 AA;  37876 MW;  91C306459209F54A CRC64;
     MQLLKDKFGR VHDYIRISVT DRCNLRCVYC MPEEGLTFLP HEKVLSKDEI VSFMELMVKF
     GIKKVRITGG EPLLRTDIVE IVRGLGAIPE IEDISITTNA MYLAKKAEAL KEAGLTRVNI
     SLDSLHADRF QAITRGGRLQ KVLDGIQKAE EVGLFPIKLN VVLIKGQNDD EITDFLQFTK
     DKDINIRFIE YMPIGHAGTS WKEKYLPLDT IFKACDDASF EYEPVDSIRG NGPSENFRIK
     GAKGTFGVIH PVSAHFCDSC NRLRLTADGY IKACLYWDEE MNIRPFIHEP VKLMQLVQKA
     IDNKPENHEM ALKLQDEVQS NKPTWRRMSQ IGG
//

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