Annotations: 1JW9

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B [auth D]	d1jw9d_	Alpha and beta proteins (a+b)	beta-Grasp (ubiquitin-like)	MoaD/ThiS	MoaD	Molybdopterin synthase subunit MoaD	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A [auth B]	d1jw9b_	Alpha and beta proteins (a/b)	Activating enzymes of the ubiquitin-like proteins	Activating enzymes of the ubiquitin-like proteins	Molybdenum cofactor biosynthesis protein MoeB	Molybdenum cofactor biosynthesis protein MoeB	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B [auth D]	SCOP2B Superfamily	MoaD/ThiS-like	8034494	3000330	SCOP2B (2022-06-29)
A [auth B]	SCOP2 Family	Molybdenum cofactor biosynthesis protein MoeB	8003472	4000181	SCOP2 (2022-06-29)
A [auth B]	SCOP2 Superfamily	Activating enzymes of the ubiquitin-like proteins	8003536	3000112	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B [auth D]	ThiS	e1jw9D1	A: a+b two layers	X: beta-Grasp	H: Ubiquitin-related	T: Ubiquitin-like	F: ThiS	ECOD (1.6)
A [auth B]	ThiF_1	e1jw9B1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Activating enzymes of the ubiquitin-like proteins	F: ThiF_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B [auth D]	3.10.20.30	Alpha Beta	Roll	Ubiquitin-like (UB roll)	Beta-grasp domain	CATH (4.3.0)
A [auth B]	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
B [auth D]	PF02597	ThiS family (ThiS)	ThiS family	ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer Swiss:O32583. ThiS is coded in the thiCEFSGH operon in E. coli. This family of proteins have two conserved Glycines at the COOH terminus. Thiocarboxylate is formed at the last G in the a ...	ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer Swiss:O32583. ThiS is coded in the thiCEFSGH operon in E. coli. This family of proteins have two conserved Glycines at the COOH terminus. Thiocarboxylate is formed at the last G in the activation process. Sulphur is transferred from ThiI to ThiS in a reaction catalysed by IscS [1]. MoaD, Swiss:P30748 a protein involved sulphur transfer in molybdopterin synthesis, is about the same length and shows limited sequence similarity to ThiS. Both have the conserved GG at the COOH end.	Domain
A [auth B]	PF00899	ThiF family (ThiF)	ThiF family	This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1 [1-3].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
B [auth D]	MOLYBDOPTERIN [MPT] CONVERTING FACTOR, SUBUNIT 1	binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding	Mo-molybdopterin cofactor biosynthetic process Mo-molybdopterin cofactor metabolic process cellular metabolic process primary metabolic process prosthetic group metabolic process molybdopterin cofactor biosynthetic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process molybdopterin cofactor metabolic process phosphate-containing compound metabolic process metabolic process cellular process protein metabolic process Mo-molybdopterin cofactor biosynthetic process Mo-molybdopterin cofactor metabolic process cellular metabolic process primary metabolic process prosthetic group metabolic process molybdopterin cofactor biosynthetic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process molybdopterin cofactor metabolic process phosphate-containing compound metabolic process metabolic process cellular process protein metabolic process macromolecule metabolic process phosphorus metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol transferase complex, transferring phosphorus-containing groups protein-containing complex catalytic complex molybdopterin adenylyltransferase complex adenylyltransferase complex transferase complex molybdopterin synthase complex sulfurtransferase complex
A [auth B]	MOLYBDOPTERIN BIOSYNTHESIS MOEB PROTEIN	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding ubiquitin-like modifier activating enzyme activity ligase activity, forming carbon-sulfur bonds catalytic activity, acting on a protein catalytic activity ligase activity ATP-dependent activity identical protein binding protein binding protein homodimerization activity protein dimerization activity adenylyltransferase activity molybdopterin-synthase adenylyltransferase activity transferase activity nucleotidyltransferase activity transferase activity, transferring phosphorus-containing groups transferase activity, transferring sulphur-containing groups sulfotransferase activity sulfurtransferase activity thiosulfate sulfurtransferase activity cation binding metal ion binding	Mo-molybdopterin cofactor biosynthetic process Mo-molybdopterin cofactor metabolic process cellular metabolic process primary metabolic process prosthetic group metabolic process molybdopterin cofactor biosynthetic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process molybdopterin cofactor metabolic process phosphate-containing compound metabolic process metabolic process cellular process protein metabolic process Mo-molybdopterin cofactor biosynthetic process Mo-molybdopterin cofactor metabolic process cellular metabolic process primary metabolic process prosthetic group metabolic process molybdopterin cofactor biosynthetic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process molybdopterin cofactor metabolic process phosphate-containing compound metabolic process metabolic process cellular process protein metabolic process macromolecule metabolic process phosphorus metabolic process	transferase complex, transferring phosphorus-containing groups protein-containing complex intracellular anatomical structure catalytic complex molybdopterin adenylyltransferase complex adenylyltransferase complex cytoplasm cellular anatomical entity transferase complex cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
B [auth D]	IPR003749	Sulfur carrier ThiS/MoaD-like	Family
B [auth D]	IPR016155	Molybdopterin synthase/thiamin biosynthesis sulphur carrier, beta-grasp	Homologous Superfamily
B [auth D]	IPR044672	Molybdopterin synthase sulfur carrier subunit	Family
B [auth D]	IPR012675	Beta-grasp domain superfamily	Homologous Superfamily
A [auth B]	IPR045886	ThiF/MoeB/HesA family	Family
A [auth B]	IPR012730	Molybdopterin synthase sulfurylase MoeB	Family
A [auth B]	IPR000594	THIF-type NAD/FAD binding fold	Domain
A [auth B]	IPR035985	Ubiquitin-activating enzyme	Homologous Superfamily

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.