P30748 (MOAD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Molybdopterin synthase sulfur carrier subunit

Alternative name(s):
MPT synthase subunit 1
Molybdenum cofactor biosynthesis protein D
Molybdopterin-converting factor small subunit
Molybdopterin-converting factor subunit 1
Sulfur carrier protein moaD

Gene names

Name:	moaD
Synonyms:	chlA4, chlM
Ordered Locus Names:	b0784, JW0767

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	81 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin. Ref.7
Pathway	Cofactor biosynthesis; molybdopterin biosynthesis.
Subunit structure	Heterotetramer of 2 moaD subunits and 2 moaE subunits. Forms a stable heterotetrameric complex of 2 moaD and 2 moeB during adenylation of moaD by moeB. During catalysis moaD shuttles between the two heterotetrameric complexes. Ref.9
Induction	By anaerobiosis, repressed by the molybdenum cofactor.
Post-translational modification	C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) by moeB, then thiocarboxylated (-COSH) by iscS.
Miscellaneous	The cross-link is not seen in all structures of the moaE-moaD complex.
Sequence similarities	Belongs to the moaD family.
Mass spectrometry	Molecular mass is 8773.6±0.2 Da from positions 1 - 81. Determined by ESI. The measured mass is that of the thiolated protein. Ref.5 Molecular mass is 8757.0±1.0 Da from positions 1 - 81. Determined by ESI. Ref.5 Molecular mass is 8744 Da from positions 1 - 81. Determined by ESI. Ref.6 Molecular mass is 8744 Da from positions 1 - 81. Determined by API. Ref.9 Molecular mass is 8760 Da from positions 1 - 81. Determined by API. The measured mass is that of the thiolated protein. Ref.9

Ontologies

Keywords
Biological process	Molybdenum cofactor biosynthesis
Ligand	Nucleotide-binding
PTM	Isopeptide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	Mo-molybdopterin cofactor biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.10Ref.11. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
moaE	P30749	3	EBI-554366,EBI-554376
moeB	P12282	3	EBI-554366,EBI-554435

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 81

81

Molybdopterin synthase sulfur carrier subunit

PRO_0000209131

Amino acid modifications

Modified residue

81

1

1-thioglycine; alternate

Modified residue

81

1

Glycyl adenylate; alternate

Cross-link

81

Glycyl lysine isopeptide (Gly-Lys) (interchain with K-119 in moaE)

Experimental info

Sequence conflict

9

1

Q → E AA sequence Ref.5

Sequence conflict

45

1

A → R in CAA49864. Ref.1

Secondary structure

1

.

.

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.

.

.

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.

.

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.

.

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.

.

81

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Helix

8 – 14

7

Beta strand

17 – 21

5

Helix

28 – 36

9

Helix

40 – 46

7

Beta strand

52 – 55

4

Beta strand

71 – 75

5

Sequences

	Sequence		Length	Mass (Da)
	P30748 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 1E0A440520EE82F4	FASTA	81	8,758
	10 20 30 40 50 60 MIKVLFFAQV RELVGTDATE VAADFPTVEA LRQHMAAQSD RWALALEDGK LLAAVNQTLV 70 80 SFDHPLTDGD EVAFFPPVTG G

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis." Rivers S.L., McNairn E., Blasco F., Giordano G., Boxer D.H. Mol. Microbiol. 8:1071-1081(1993) [PubMed: 8361352] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[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]	"The biosynthesis of molybdopterin in Escherichia coli. Purification and characterization of the converting factor." Pitterle D.M., Rajagopalan K.V. J. Biol. Chem. 268:13499-13505(1993) [PubMed: 8514782] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15, CHARACTERIZATION, MASS SPECTROMETRY, IDENTIFICATION OF THIOCARBOXYLATE.
[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: IDENTIFICATION OF ACYL ADENYLATE MODIFICATION, INTERACTION WITH MOEB, MASS SPECTROMETRY. Strain: K12 / DH5-alpha.
[7]	"Role of the C-terminal Gly-Gly motif of Escherichia coli MoaD, a molybdenum cofactor biosynthesis protein with a ubiquitin fold." Schmitz J., Wuebbens M.M., Rajagopalan K.V., Leimkuehler S. Biochemistry 46:909-916(2007) [PubMed: 17223713] [Abstract] Cited for: FUNCTION.
[8]	"IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli." Zhang W., Urban A., Mihara H., Leimkuehler S., Kurihara T., Esaki N. J. Biol. Chem. 285:2302-2308(2010) [PubMed: 19946146] [Abstract] Cited for: IDENTIFICATION OF ISCS AS SULFUR DONOR, INTERACTION WITH ISCS.
[9]	"Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation." Rudolph M.J., Wuebbens M.M., Rajagopalan K.V., Schindelin H. Nat. Struct. Biol. 8:42-46(2001) [PubMed: 11135669] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMLEXES WITH MOAE, CROSS-LINKING TO MOAE, MASS SPECTROMETRY, SUBUNIT.
[10]	"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 MOEB; ZINC; ATP AND IN AN ADENYLATE FORM, COVALENT BINDING OF AMP.
[11]	"Structural studies of molybdopterin synthase provide insights into its catalytic mechanism." Rudolph M.J., Wuebbens M.M., Turque O., Rajagopalan K.V., Schindelin H. J. Biol. Chem. 278:14514-14522(2003) [PubMed: 12571227] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF THIOCARBOXYLATE FORM IN COMPLEX WITH MOAE, THIOCARBOXYLATION AT GLY-81, REACTION MECHANISM.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X70420 Genomic DNA. Translation: CAA49864.1.
U00096 Genomic DNA. Translation: AAC73871.1.
AP009048 Genomic DNA. Translation: BAA35442.1.

PIR

H64814.

RefSeq

NP_415305.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FM0	X-ray	1.45	D	1-81	[»]
1FMA	X-ray	1.58	D	1-81	[»]
1JW9	X-ray	1.70	D	1-81	[»]
1JWA	X-ray	2.90	D	1-81	[»]
1JWB	X-ray	2.10	D	1-81	[»]
1NVI	X-ray	1.90	D	3-81	[»]
3BII	X-ray	2.50	D	1-81	[»]

ProteinModelPortal

P30748.

SMR

P30748. Positions 1-81.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10231N.

IntAct

P30748. 13 interactions.

MINT

MINT-155528.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001553; EBESCP00000001553; EBESCG00000001290.
EBESCT00000001554; EBESCP00000001554; EBESCG00000001290.
EBESCT00000001555; EBESCP00000001555; EBESCG00000001290.
EBESCT00000016441; EBESCP00000015732; EBESCG00000015501.

GeneID

945398.

GenomeReviews

Gene locus JW0767 in contig AP009048_GR.
Gene locus b0784 in contig U00096_GR.

KEGG

ecj:JW0767.
eco:b0784.

PATRIC

32116769. VBIEscCol129921_0810.

Organism-specific databases

EchoBASE

EB1554.

EcoGene

EG11597. moaD.

Phylogenomic databases

eggNOG

COG1977.

GeneTree

EBGT00050000009981.

HOGENOM

HBG690308.

OMA

AEQNLMC.

PhylomeDB

P30748.

ProtClustDB

PRK11130.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11597-MONOMER.
MetaCyc:EG11597-MONOMER.

Gene expression databases

Genevestigator

P30748.

Family and domain databases

InterPro

IPR012675. Beta-grasp_ferredoxin-type.
IPR010034. Mopterin_su_1.
IPR016155. Mopterin_synth/thiamin_S_b.
IPR003749. ThiS.
[Graphical view]

Gene3D

G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.

KO

K03636.

Pfam

PF02597. ThiS. 1 hit.
[Graphical view]

SUPFAM

SSF54285. Mo_synth/thiamin_syn_S_b-grasp. 1 hit.

TIGRFAMs

TIGR01682. MoaD. 1 hit.

ProtoNet

Search...

Entry information

Entry name

MOAD_ECOLI

Accession

Primary (citable) accession number: P30748
Secondary accession number(s): P77422

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program