Q9FV52 (AMP1B_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Methionine aminopeptidase 1B, chloroplastic
Short name=MAP 1B
Short name=MetAP 1B
EC=3.4.11.18

Alternative name(s):
Peptidase M 1B

Gene names

Name:	MAP1B
Ordered Locus Names:	At1g13270
ORF Names:	T6J4.3

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Removes the amino-terminal methionine from nascent proteins By similarity.
Catalytic activity	Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Cofactor	Binds 2 cobalt ions per subunit. The true nature of the physiological cofactor is under debate. The enzyme is also active with zinc, manganese or divalent iron ions By similarity.
Subcellular location	Plastid › chloroplast Ref.1.
Tissue specificity	Ubiquitous. Preferentially expressed in green tissues. Ref.1
Sequence similarities	Belongs to the peptidase M24A family.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	Cobalt Metal-binding
Molecular function	Aminopeptidase Hydrolase Protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	N-terminal protein amino acid modification Traceable author statement. Source: TAIR proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from direct assay. Source: TAIR mitochondrion Traceable author statement. Source: TAIR
Molecular function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metalloexopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9FV52-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 55	55	Chloroplast Potential
	Chain	56 – 369	314	Methionine aminopeptidase 1B, chloroplastic		PRO_0000045805
Sites
	Metal binding	216	1	Cobalt 1 By similarity
	Metal binding	227	1	Cobalt 1 By similarity
	Metal binding	227	1	Cobalt 2 By similarity
	Metal binding	290	1	Cobalt 2 By similarity
	Metal binding	322	1	Cobalt 2 By similarity
	Metal binding	353	1	Cobalt 1 By similarity
	Metal binding	353	1	Cobalt 2 By similarity
	Binding site	199	1	Substrate By similarity
	Binding site	297	1	Substrate By similarity
Experimental info
	Sequence conflict	34	1	L → I in AAG33975. Ref.1
	Sequence conflict	243	1	R → Q in AAG33975. Ref.1
	Sequence conflict	254	1	R → K in AAG33975. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 24, 2006. Version 2. Checksum: 0D28974852F33747	FASTA	369	40,424
	10 20 30 40 50 60 MASSVFLSSF SSSSSLQLCS SFHGEYLAPS RCFLGAPVTS SSLSLSGKKN SYSPRQFHVS 70 80 90 100 110 120 AKKVSGLEEA IRIRKMRELE TKSKVRRNPP LRRGRVSPRL LVPDHIPRPP YVESGVLPDI 130 140 150 160 170 180 SSEFQIPGPE GIAKMRAACE LAARVLNYAG TLVKPSVTTN EIDKAVHDMI IEAGAYPSPL 190 200 210 220 230 240 GYGGFPKSVC TSVNECMCHG IPDSRQLQSG DIINIDVTVY LDGYHGDTSR TFFCGEVDEG 250 260 270 280 290 300 FKRLVKVTEE CLERGIAVCK DGASFKKIGK RISEHAEKFG YNVVERFVGH GVGPVFHSEP 310 320 330 340 350 360 LIYHYRNDEP GLMVEGQTFT IEPILTIGTT ECVTWPDNWT TLTADGGVAA QFEHTILITR TGSEILTKC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms." Giglione C., Serero A., Pierre M., Boisson B., Meinnel T. EMBO J. 19:5916-5929(2000) [PubMed: 11060042] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF250961 mRNA. Translation: AAG33975.1. AC011810 Genomic DNA. Translation: AAG09564.1. CP002684 Genomic DNA. Translation: AEE28993.1. BT000449 mRNA. Translation: AAN17426.1. BT001213 mRNA. Translation: AAN65100.1.
IPI	IPI00549091.
PIR	C86267.
RefSeq	NP_172785.1. NM_101198.3.
UniGene	At.21097.
3D structure databases
ProteinModelPortal	Q9FV52.
SMR	Q9FV52. Positions 89-368.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9FV52.
Protein family/group databases
MEROPS	M24.A05.
Proteomic databases
PRIDE	Q9FV52.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G13270.1; AT1G13270.1; AT1G13270.
GeneID	837887.
GenomeReviews	Gene locus AT1G13270 in contig CT485782_GR.
KEGG	ath:AT1G13270.
NMPDR	fig|3702.1.peg.1597.
Organism-specific databases
GeneFarm	2345. 184.
TAIR	At1g13270.
Phylogenomic databases
GeneTree	EPGT00050000011147.
HOGENOM	HBG299384.
InParanoid	Q9FV52.
OMA	FHENPYV.
PhylomeDB	Q9FV52.
ProtClustDB	CLSN2682512.
Gene expression databases
Genevestigator	Q9FV52.
Family and domain databases
InterPro	IPR001714. Pept_M24_MAP. IPR000994. Pept_M24_structural-domain. IPR002467. Pept_M24A_MAP1. [Graphical view]
Gene3D	G3DSA:3.90.230.10. Peptidase_M24_cat_core. 1 hit.
KO	K01265.
Pfam	PF00557. Peptidase_M24. 1 hit. [Graphical view]
PRINTS	PR00599. MAPEPTIDASE.
SUPFAM	SSF55920. Peptidase_M24_cat_core. 1 hit.
TIGRFAMs	TIGR00500. Met_pdase_I. 1 hit.
PROSITE	PS00680. MAP_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMP1B_ARATH

Accession

Primary (citable) accession number: Q9FV52
Secondary accession number(s): Q9FX70

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2006
Last sequence update:	January 24, 2006
Last modified:	November 16, 2011
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program