ID   MOEB_HAEIN              Reviewed;         243 AA.
AC   P45211;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 136.
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; Synonyms=chlN; OrderedLocusNames=HI_1449;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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   -!- 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; L42023; AAC23099.1; -; Genomic_DNA.
DR   PIR; C64124; C64124.
DR   RefSeq; NP_439601.1; NC_000907.1.
DR   RefSeq; WP_005693917.1; NC_000907.1.
DR   AlphaFoldDB; P45211; -.
DR   SMR; P45211; -.
DR   STRING; 71421.HI_1449; -.
DR   EnsemblBacteria; AAC23099; AAC23099; HI_1449.
DR   KEGG; hin:HI_1449; -.
DR   PATRIC; fig|71421.8.peg.1511; -.
DR   eggNOG; COG0476; Bacteria.
DR   HOGENOM; CLU_013325_10_3_6; -.
DR   OMA; LGSWEVY; -.
DR   PhylomeDB; P45211; -.
DR   BioCyc; HINF71421:G1GJ1-1475-MON; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000579; 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: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; Molybdenum cofactor biosynthesis; Nucleotide-binding;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..243
FT                   /note="Molybdopterin-synthase adenylyltransferase"
FT                   /id="PRO_0000120577"
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"
SQ   SEQUENCE   243 AA;  26997 MW;  218A3382A975BDBD CRC64;
     MIELSHEEEL RYNRQIILKS VDFDGQEKLK ASKMLIVGLG GLGCAASQYL AAAGVGNLTL
     LDFDTVSLSN LQRQVLHCDA RLNMPKVESA KIALEQINPH INIETINAKL DEEKLAEIIP
     HFDIVLDCTD NVEIRNQLDR QCNHMKVPLI SGAAIRMEGQ VSVFTYEPNT PTYRDLSKLF
     RQNVLSCVEA GVLAPIVGIV GCIQALEAIK VRLKIGKNLC GRLLMIDGFS MNIREIKLPT
     NME