ID   MOEB_GRATL              Reviewed;         355 AA.
AC   Q6B908;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
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; OrderedLocusNames=Grc000046;
OS   Gracilaria tenuistipitata var. liui (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC   Gracilariaceae; Agarophyton; Agarophyton tenuistipitatum.
OX   NCBI_TaxID=285951;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15638458; DOI=10.1007/s00239-004-2638-3;
RA   Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., de Oliveira M.C.;
RT   "Comparative analysis of the complete plastid genome sequence of the red
RT   alga Gracilaria tenuistipitata var. liui provides insights into the
RT   evolution of rhodoplasts and their relationship to other plastids.";
RL   J. Mol. Evol. 59:464-477(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY673996; AAT79627.1; -; Genomic_DNA.
DR   RefSeq; YP_063552.1; NC_006137.1.
DR   AlphaFoldDB; Q6B908; -.
DR   SMR; Q6B908; -.
DR   GeneID; 2944035; -.
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..355
FT                   /note="Probable molybdopterin-synthase adenylyltransferase"
FT                   /id="PRO_0000277343"
FT   DOMAIN          277..355
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   BINDING         47
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         75..79
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         136..137
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   355 AA;  40669 MW;  9562A282AC520B42 CRC64;
     MSYSITNSSL SELEYKKYAR HLVLDNIGDS GQKRLKAAKI LFIGAGGLAA SAILYLAASG
     VNCLGVADDD KVDYSNLHRQ ILYNNKDVGK LKVGIVYDRI KMINPECNVN VYSSLVDEYN
     CEYIIKNYDI VIDTTDNFQS RYIISKSCYL QHKVHIYGAV RGFEGHISVF NYRSGPIYSD
     LYPQSLNLDV KECNMFGVLG VTTGIIGIFQ AVEAMKVILG IGNILSGYLL VYNLLDASFK
     KFKILPKNNI NVAHYHFNNQ FAYCNIISEQ DLSLIRSKYK IILIDVRQPE EFIKHHLLKA
     INIPLKNIRS RKNMYFMRDF LIDKIIIVYC YDNLRSLIAS QILYKHRISH YLLNY