P12282 (MOEB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sulfur carrier protein moaD adenylyltransferase
EC=2.7.7.n4

Alternative name(s):
MoaD protein adenylase
Molybdopterin-converting factor subunit 1 adenylase

Gene names

Name:	moeB
Synonyms:	chlN
Ordered Locus Names:	b0826, JW0810

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	249 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein moaD. Ref.5 Ref.6
Catalytic activity	ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly = AMP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP + diphosphate. Ref.6
Cofactor	Binds 1 zinc ion per subunit. Ref.6
Pathway	Cofactor biosynthesis; molybdopterin biosynthesis.
Subunit structure	Homodimer. Forms a stable heterotetrameric complex of 2 moeB and 2 moaD during adenylation of moaD. Ref.6
Sequence similarities	Belongs to the hesA/moeB/thiF family.
Mass spectrometry	Molecular mass is 26563 Da from positions 1 - 249. Determined by ESI. Ref.6

Ontologies

Keywords
Biological process	Molybdenum cofactor biosynthesis
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	Mo-molybdopterin cofactor biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotidyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.7. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
moaD	P30748	3	EBI-554435,EBI-554366

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 249

249

Sulfur carrier protein moaD adenylyltransferase

PRO_0000120575

Regions

Nucleotide binding

69 – 73

5

ATP

Nucleotide binding

130 – 131

2

ATP

Sites

Metal binding

172

1

Zinc

Metal binding

175

1

Zinc

Metal binding

244

1

Zinc

Metal binding

247

1

Zinc

Binding site

41

1

ATP; via amide nitrogen

Binding site

62

1

ATP

Binding site

86

1

ATP

Experimental info

Mutagenesis

14

1

R → A or K: No effect. Ref.7

Mutagenesis

14

1

R → A: No activity; when associated with A-73. Ref.7

Mutagenesis

44

1

C → A: No effect. Ref.6

Mutagenesis

73

1

R → A: No effect. No activity; when associated with A-14. Ref.7

Mutagenesis

73

1

R → K: Substantially reduced activity. Ref.7

Mutagenesis

128

1

C → A: No effect. Ref.6

Mutagenesis

128

1

C → Y: No activity. Ref.6

Mutagenesis

130

1

D → A: No activity. Ref.7

Mutagenesis

130

1

D → E: Substantially reduced activity. Ref.7

Mutagenesis

142

1

C → A: No effect. Ref.6

Mutagenesis

172

1

C → A: No zinc bound and no enzyme activity. Ref.6

Mutagenesis

175

1

C → A: No zinc bound and no enzyme activity. Ref.6

Mutagenesis

187

1

C → A: No effect. Ref.6

Mutagenesis

231

1

C → A: No effect. Ref.6

Mutagenesis

244

1

C → A: No zinc bound and almost no enzyme activity. Ref.6

Mutagenesis

247

1

C → A: No zinc bound and almost no enzyme activity. Ref.6

Secondary structure

1

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249

Helix Strand Turn

Details...

Helix

6 – 11

6

Helix

13 – 16

4

Turn

19 – 21

3

Helix

22 – 31

10

Beta strand

33 – 37

5

Helix

41 – 53

13

Beta strand

56 – 61

6

Helix

68 – 72

5

Helix

79 – 81

3

Helix

86 – 97

12

Beta strand

101 – 106

6

Helix

112 – 120

9

Beta strand

122 – 127

6

Helix

132 – 145

14

Beta strand

149 – 156

8

Beta strand

158 – 164

7

Helix

173 – 177

5

Helix

194 – 213

20

Beta strand

220 – 227

8

Turn

228 – 231

4

Beta strand

232 – 237

6

Turn

245 – 247

3

Sequences

	Sequence		Length	Mass (Da)
	P12282 [UniParc]. Last modified October 1, 1989. Version 1. Checksum: 12C77082B3F39D7D	FASTA	249	26,719
	10 20 30 40 50 60 MAELSDQEML RYNRQIILRG FDFDGQEALK DSRVLIVGLG GLGCAASQYL ASAGVGNLTL 70 80 90 100 110 120 LDFDTVSLSN LQRQTLHSDA TVGQPKVESA RDALTRINPH IAITPVNALL DDAELAALIA 130 140 150 160 170 180 EHDLVLDCTD NVAVRNQLNA GCFAAKVPLV SGAAIRMEGQ ITVFTYQDGE PCYRCLSRLF 190 200 210 220 230 240 GENALTCVEA GVMAPLIGVI GSLQAMEAIK MLAGYGKPAS GKIVMYDAMT CQFREMKLMR NPGCEVCGQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of the Escherichia coli chlEN operon involved in molybdopterin biosynthesis." Nohno T., Kasai Y., Saito T. J. Bacteriol. 170:4097-4102(1988) [PubMed: 3045084] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ZK126.
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli." Leimkuehler S., Rajagopalan K.V. J. Biol. Chem. 276:22024-22031(2001) [PubMed: 11290749] [Abstract] Cited for: FUNCTION, SULFUR DONOR.
[6]	"Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor." Leimkuehler S., Wuebbens M.M., Rajagopalan K.V. J. Biol. Chem. 276:34695-34701(2001) [PubMed: 11463785] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, INTERACTION WITH MOAD, MUTAGENESIS OF CYS-44; CYS-128; CYS-142; CYS-172; CYS-175; CYS-187; CYS-231; CYS-244 AND CYS-247, MASS SPECTROMETRY. Strain: K12 / DH5-alpha.
[7]	"Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex." Lake M.W., Wuebbens M.M., Rajagopalan K.V., Schindelin H. Nature 414:325-329(2001) [PubMed: 11713534] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH MOAD; ZINC; MOAD AND ATP AND MOAD-ADENYLATE, MUTAGENESIS OF ARG-14; ARG-73 AND ASP-130, REACTION MECHANISM.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M21151 Genomic DNA. Translation: AAA23580.1.
U00096 Genomic DNA. Translation: AAC73913.1.
AP009048 Genomic DNA. Translation: BAA35514.1.

PIR

B32352.

RefSeq

NP_415347.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JW9	X-ray	1.70	B	1-249	[»]
1JWA	X-ray	2.90	B	1-249	[»]
1JWB	X-ray	2.10	B	1-249	[»]

ProteinModelPortal

P12282.

SMR

P12282. Positions 2-248.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10241N.

IntAct

P12282. 15 interactions.

MINT

MINT-222244.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000004863; EBESCP00000004863; EBESCG00000003968.
EBESCT00000014359; EBESCP00000013650; EBESCG00000013420.

GeneID

945452.

GenomeReviews

Gene locus JW0810 in contig AP009048_GR.
Gene locus b0826 in contig U00096_GR.

KEGG

ecj:JW0810.
eco:b0826.

PATRIC

32116855. VBIEscCol129921_0853.

Organism-specific databases

EchoBASE

EB0152.

EcoGene

EG10154. moeB.

Phylogenomic databases

eggNOG

COG0476.

GeneTree

EBGT00050000010430.

HOGENOM

HBG535305.

OMA

DFDGQET.

PhylomeDB

P12282.

ProtClustDB

PRK05690.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10154-MONOMER.
MetaCyc:EG10154-MONOMER.

Gene expression databases

Genevestigator

P12282.

Family and domain databases

InterPro

IPR007901. MoeZ_MoeB.
IPR009036. Molybdenum_cofac_synth_MoeB.
IPR012730. Mopterin_Synthase_Sase_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

KO

K11996.

Pfam

PF05237. MoeZ_MoeB. 1 hit.
PF00899. ThiF. 1 hit.
[Graphical view]

SUPFAM

SSF69572. MoeB. 1 hit.

TIGRFAMs

TIGR02355. MoeB. 1 hit.

ProtoNet

Search...

Entry information

Entry name

MOEB_ECOLI

Accession

Primary (citable) accession number: P12282

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	October 1, 1989
Last modified:	January 25, 2012
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program