MOCBA_SYNY3
ID MOCBA_SYNY3 Reviewed; 347 AA.
AC Q55370;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Molybdenum cofactor biosynthesis bifunctional protein;
DE Includes:
DE RecName: Full=Cyclic pyranopterin monophosphate synthase {ECO:0000250|UniProtKB:P0A738};
DE EC=4.6.1.17 {ECO:0000250|UniProtKB:P0A738};
DE AltName: Full=Molybdenum cofactor biosynthesis protein C {ECO:0000250|UniProtKB:P0A738};
DE Includes:
DE RecName: Full=Probable molybdenum cofactor guanylyltransferase;
DE Short=MoCo guanylyltransferase;
DE EC=2.7.7.77;
DE AltName: Full=GTP:molybdopterin guanylyltransferase;
DE AltName: Full=Mo-MPT guanylyltransferase;
DE AltName: Full=Molybdopterin guanylyltransferase;
DE AltName: Full=Molybdopterin-guanine dinucleotide synthase;
DE Short=MGD synthase;
GN Name=moaC/mobA; OrderedLocusNames=slr0902;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-
CC dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate
CC (cPMP). {ECO:0000250|UniProtKB:P0A738}.
CC -!- FUNCTION: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT)
CC cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine
CC dinucleotide (Mo-MGD) cofactor. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin
CC guanine dinucleotide; Xref=Rhea:RHEA:34243, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:71302,
CC ChEBI:CHEBI:71310; EC=2.7.7.77;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic
CC pyranopterin phosphate + diphosphate; Xref=Rhea:RHEA:49580,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:59648, ChEBI:CHEBI:131766;
CC EC=4.6.1.17; Evidence={ECO:0000250|UniProtKB:P0A738};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The N-terminal domain of the MobA region determines nucleotide
CC recognition and specific binding, while its C-terminal domain
CC determines the specific binding to the target protein. {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MoaC family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MobA family.
CC {ECO:0000305}.
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DR EMBL; BA000022; BAA10452.1; -; Genomic_DNA.
DR PIR; S75717; S75717.
DR AlphaFoldDB; Q55370; -.
DR SMR; Q55370; -.
DR STRING; 1148.1001212; -.
DR PaxDb; Q55370; -.
DR EnsemblBacteria; BAA10452; BAA10452; BAA10452.
DR KEGG; syn:slr0902; -.
DR eggNOG; COG0315; Bacteria.
DR eggNOG; COG0746; Bacteria.
DR InParanoid; Q55370; -.
DR OMA; CAIYTPQ; -.
DR PhylomeDB; Q55370; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061603; F:molybdenum cofactor guanylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01420; MoaC_PE; 1.
DR CDD; cd02503; MobA; 1.
DR Gene3D; 3.30.70.640; -; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR HAMAP; MF_00316; MobA; 1.
DR InterPro; IPR023045; Mo_CF_biosynth-C.
DR InterPro; IPR036522; MoaC_sf.
DR InterPro; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR013482; Molybde_CF_guanTrfase.
DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01967; MoaC; 1.
DR Pfam; PF12804; NTP_transf_3; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR SUPFAM; SSF55040; SSF55040; 1.
DR TIGRFAMs; TIGR00581; moaC; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Lyase; Magnesium; Metal-binding;
KW Molybdenum cofactor biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..347
FT /note="Molybdenum cofactor biosynthesis bifunctional
FT protein"
FT /id="PRO_0000134926"
FT REGION 1..158
FT /note="Molybdenum cofactor biosynthesis protein C"
FT REGION 159..347
FT /note="Molybdenum cofactor guanylyltransferase"
FT ACT_SITE 131
FT /note="For MoaC activity"
FT /evidence="ECO:0000255"
FT BINDING 75..77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A738"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A738"
FT BINDING 167..169
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 347 AA; 38380 MW; 7757A1BAC5C2C858 CRC64;
MFTHLDENQQ PRMVDISQKV AGDRRAVAQC IVQLPKAIKD YLTGQEIFLK KGPVIQTAII
AGTMAVKKTA DLIPFCHTLP IHGCKFDINI VYQKRDYLEI FLQCAVNTNY KTGVEMEALC
GVSVAALTIY DMCKSISSEI IIKNTKLIEK TGGKADVSQT PLYGLVLTGG KSRRMGKDKA
LINYQGQPHG QYIYDLLAKY CEQVFLSARP SQWQGTPLEN LPTLVDRGES VGPMSGILTA
LQSYPGVNWL IIACDLAYIN STMVEKLIAQ ARQDLVATCY ENADQGFPEA LCGFYTPLAL
QLFTKAQNIG LHCPVKILQM ADCQLIKPDN LFDIANINSP EDYGQIN
