Reviewed, UniProtKB/Swiss-Prot P0A738 (MOAC_ECOLI)

Names and origin

Protein names

Recommended name:
    Molybdenum cofactor biosynthesis protein C

Gene names

Name:	moaC
Synonyms:	chlA3
Ordered Locus Names:	b0783, JW0766

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	161 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Together with moaA, is involved in the conversion of a guanosine derivative (5'-GTP) into molybdopterin precursor Z. HAMAP MF_01224
Pathway	Cofactor biosynthesis; molybdopterin biosynthesis. HAMAP MF_01224
Subunit structure	Homohexamer. HAMAP MF_01224
Induction	By anaerobiosis, repressed by the molybdenum cofactor. HAMAP MF_01224
Sequence similarities	Belongs to the moaC family.

Ontologies

Keywords
Biological process	Molybdenum cofactor biosynthesis
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	Mo-molybdopterin cofactor biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
rplA	P0A7L0	1	EBI-554314,EBI-543771

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 161

160

Molybdenum cofactor biosynthesis protein C HAMAP MF_01224

PRO_0000097798

Sites

Active site

128

1

Potential

Experimental info

Mutagenesis

51

1

K → A: Reduced activity. Ref.5

Mutagenesis

52

1

G → A: Reduced activity. Ref.5

Mutagenesis

67

1

K → A: Reduced activity. Ref.5

Mutagenesis

76

1

C → A: Reduced activity. Ref.5

Mutagenesis

77

1

H → A: Reduced activity. Ref.5

Mutagenesis

110

1

G → A: Reduced activity. Ref.5

Mutagenesis

112

1

E → A: Reduced activity. Ref.5

Mutagenesis

117

1

T → P: Strongly reduced activity. Ref.5

Mutagenesis

128

1

D → A: Loss of activity. Ref.5

Mutagenesis

131

1

K → A: Reduced activity. Ref.5

Sequence conflict

17

1

D → N in CAA49863. Ref.1

Sequence conflict

92 – 97

6

PEHNRV → RAQSG in CAA49863. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

161

Helix Strand Turn

Details...

Beta strand

24 – 35

12

Helix

38 – 45

8

Helix

54 – 67

14

Helix

69 – 72

4

Beta strand

82 – 91

10

Helix

92 – 94

3

Beta strand

96 – 109

14

Helix

112 – 130

19

Helix

131 – 133

3

Beta strand

138 – 147

10

Sequences

	Sequence		Length	Mass (Da)
	P0A738-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 280DAC1EFAAA04AD	FASTA	161	17,467
	10 20 30 40 50 60 MSQLTHINAA GEAHMVDVSA KAETVREARA EAFVTMRSET LAMIIDGRHH KGDVFATARI 70 80 90 100 110 120 AGIQAAKRTW DLIPLCHPLM LSKVEVNLQA EPEHNRVRIE TLCRLTGKTG VEMEALTAAS 130 140 150 160 VAALTIYDMC KAVQKDMVIG PVRLLAKSGG KSGDFKVEAD D

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], PROTEIN SEQUENCE OF 2-11. 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]	"Insights into molybdenum cofactor deficiency provided by the crystal structure of the molybdenum cofactor biosynthesis protein MoaC." Wuebbens M.M., Liu M.T.W., Rajagopalan K.V., Schindelin H. Structure 8:709-718(2000) [PubMed: 10903949] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), MUTAGENESIS OF LYS-51; GLY-52; LYS-67; CYS-76; HIS-77; GLY-110; GLU-112; THR-117; ASP-128 AND LYS-131.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X70420 Genomic DNA. Translation: CAA49863.1.
U00096 Genomic DNA. Translation: AAC73870.1.
AP009048 Genomic DNA. Translation: BAA35441.1.

PIR

G64814.

RefSeq

AP_001414.1.
NP_415304.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EKR	X-ray	2.00	A	3-161	[»]
1EKS	X-ray	2.50	A	3-161	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A738. 20 interactions.

STRING

P0A738.

Genome annotation databases

GeneID

945397.

GenomeReviews

Gene locus JW0766 in contig AP009048_GR.
Gene locus b0783 in contig U00096_GR.

KEGG

ecj:JW0766.
eco:b0783.

Organism-specific databases

EchoBASE

EB1617.

EcoGene

EG11666. moaC.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A738.

OMA

MGAKKTS

Enzyme and pathway databases

BioCyc

EcoCyc:EG11666-MON.
ECOL168927:B0783-MON.

Gene expression databases

Genevestigator

P0A738.

Family and domain databases

HAMAP

MF_01224.
[Tree]

InterPro

IPR002820. Mopterin_CF_MoaC_reg.
[Graphical view]

Gene3D

G3DSA:3.30.70.640. MoaC_reg. 1 hit.

Pfam

PF01967. MoaC. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00581. moaC. 1 hit.

ProtoNet

Search...

Entry information

Entry name

MOAC_ECOLI

Accession

Primary (citable) accession number: P0A738
Secondary accession number(s): P30747, P77530

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	January 23, 2007
Last modified:	November 24, 2009
This is version 48 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)