ID   MOEB_PORPU              Reviewed;         382 AA.
AC   P51335;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Probable 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;
OS   Porphyra purpurea (Red seaweed) (Ulva purpurea).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX   NCBI_TaxID=2787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Avonport;
RA   Reith M.E., Munholland J.;
RT   "Complete nucleotide sequence of the Porphyra purpurea chloroplast
RT   genome.";
RL   Plant Mol. Biol. Rep. 13:333-335(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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the HesA/MoeB/ThiF family. {ECO:0000305}.
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DR   EMBL; U38804; AAC08221.1; -; Genomic_DNA.
DR   PIR; S73256; S73256.
DR   RefSeq; NP_053945.1; NC_000925.1.
DR   AlphaFoldDB; P51335; -.
DR   SMR; P51335; -.
DR   GeneID; 809970; -.
DR   UniPathway; UPA00344; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.250.10; -; 1.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
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; PF00581; Rhodanese; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF69572; SSF69572; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chloroplast; Molybdenum cofactor biosynthesis;
KW   Nucleotide-binding; Nucleotidyltransferase; Plastid; Transferase.
FT   CHAIN           1..382
FT                   /note="Probable molybdopterin-synthase adenylyltransferase"
FT                   /id="PRO_0000120574"
FT   DOMAIN          288..377
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   BINDING         48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         76..80
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         137..138
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   382 AA;  43374 MW;  D931A7A68B5AF385 CRC64;
     MLNFRAKCTT YSLEEYTRYS KHLILPQIKL EGQERLKQSS ILCVGAGGLG SPALIYLAAS
     GIGKIGIVDN DIIDISNLQR QILYTVNDIG LSKAYIAKKK ILEINPTCNV QIFNTRLQSI
     NAIEIIRQYD IIIDGTDNFG SRYIISDSCL ELNKIHIYGA IFQFEGQVST FNYQGGPKYR
     DFHNNIETEN NPEDTCSNAG VLGLLPGIIG TLQATEAIKI ILGYKSVLSG IILKYNAMTI
     SFEKFKIIHT QFILSQPKKK IKSLLVGNSS YPVQEIDVIE LQNELYRNSF KYIILDVRSK
     EEYEESHLDK AVNLPIKDMK KRYYSDLNLQ DKISFIYCSV DSRSIFAYNF LRKQEFKVIR
     VKGGLSSWTN IIGNEKLYVK SC