ID   MOEB_NEOYE              Reviewed;         378 AA.
AC   Q1XDF1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 61.
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   Neopyropia yezoensis (Susabi-nori) (Pyropia yezoensis).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Neopyropia.
OX   NCBI_TaxID=2788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U-51;
RA   Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA   Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT   "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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; AP006715; BAE92460.1; -; Genomic_DNA.
DR   RefSeq; YP_537017.1; NC_007932.1.
DR   AlphaFoldDB; Q1XDF1; -.
DR   SMR; Q1XDF1; -.
DR   GeneID; 3978798; -.
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..378
FT                   /note="Probable molybdopterin-synthase adenylyltransferase"
FT                   /id="PRO_0000277344"
FT   DOMAIN          287..376
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   378 AA;  43004 MW;  3F8D9A20241C97E7 CRC64;
     MLNFKTENTK YSLEEYTRYS KHLVLPQIQL EGQERLKEAK VLFIGAGGLG SPGIIYLAAA
     GIGSIGIIDD DIIDLSNLQR QILYRCNDIG YSKVEIAKKK ILDLNPQCIV TVFKTRLSYE
     NSIDIIRQYD IIIDGSDNFD TRYLLNDTCL ELNKIHIYGA IFQFEGQVSV FNYQGGPVYR
     DFYSETENKE SARDTCSNSG VLGLLPGIVG TLQATEAVKI VLGYKSILSG TILTYNSLTS
     SFNKFKIINT KFVLSTKKHW NKYYGSKSST FVREISVIQL QKFLISRNPQ YILIDVRNHE
     EYHKSHLIHS LNLPLQKIKG MNYSHINLQD KICFVYCSLD SRSIFASKFL IAQKLNIVRV
     RGGLNAWKNI IGDLDWTL