MOEB_SALTY
ID MOEB_SALTY Reviewed; 249 AA.
AC Q56067;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Molybdopterin-synthase adenylyltransferase;
DE EC=2.7.7.80;
DE AltName: Full=MoaD protein adenylase;
DE AltName: Full=Molybdopterin-converting factor subunit 1 adenylase;
DE AltName: Full=Sulfur carrier protein MoaD adenylyltransferase;
GN Name=moeB; OrderedLocusNames=STM0845;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RA Wong K.K., Kwan H.S.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Catalyzes the adenylation by ATP of the carboxyl group of the
CC C-terminal glycine of sulfur carrier protein MoaD. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal
CC Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier
CC protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616,
CC Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618,
CC ChEBI:CHEBI:90778; EC=2.7.7.80;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- SUBUNIT: Homodimer. Forms a stable heterotetrameric complex of 2 MoeB
CC and 2 MoaD during adenylation of MoaD (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HesA/MoeB/ThiF family. {ECO:0000305}.
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DR EMBL; U53178; AAA96530.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19781.1; -; Genomic_DNA.
DR RefSeq; NP_459822.1; NC_003197.2.
DR RefSeq; WP_000829280.1; NC_003197.2.
DR AlphaFoldDB; Q56067; -.
DR SMR; Q56067; -.
DR STRING; 99287.STM0845; -.
DR PaxDb; Q56067; -.
DR PRIDE; Q56067; -.
DR EnsemblBacteria; AAL19781; AAL19781; STM0845.
DR GeneID; 1252364; -.
DR KEGG; stm:STM0845; -.
DR PATRIC; fig|99287.12.peg.882; -.
DR HOGENOM; CLU_013325_10_3_6; -.
DR OMA; MIYDALE; -.
DR PhylomeDB; Q56067; -.
DR BioCyc; SENT99287:STM0845-MON; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061605; F:molybdopterin-synthase adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR012730; Mopterin_Synthase_Sase_MoeB.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; PTHR10953; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; SSF69572; 1.
DR TIGRFAMs; TIGR02355; moeB; 1.
PE 3: Inferred from homology;
KW ATP-binding; Metal-binding; Molybdenum cofactor biosynthesis;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase; Zinc.
FT CHAIN 1..249
FT /note="Molybdopterin-synthase adenylyltransferase"
FT /id="PRO_0000120576"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 69..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 130..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 9
FT /note="M -> I (in Ref. 1; AAA96530)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="G -> R (in Ref. 1; AAA96530)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="S -> A (in Ref. 1; AAA96530)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="N -> T (in Ref. 1; AAA96530)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="G -> E (in Ref. 1; AAA96530)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 26903 MW; 0F0050831D537AD2 CRC64;
MAELSDQEML RYNRQIILRG FDFEGQEALK DARVLVVGLG GLGCAATQYL AGAGVGQLTL
LDFDTVSVSN LQRQTLHSDA TVGQPKVESA RDALARINPH ITITPVNARL DDDAMTSLIA
GHSLVLDCTD NVSVRNQLNA GCYTAKVPLI SGAAIRMEGQ VTVFTYRENE PCYRCLSRLF
GENALTCVEA GVMAPLIGVI GSLQAMEAIK LLAHYGQPAS GKIVMYDAMT CQFREMKLMR
NPGCEVCGQ
