P45632 (EXOC_AZOBR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphomannomutase
Short name=PMM
EC=5.4.2.8

Gene names

Name:

exoC

Organism

Azospirillum brasilense

Taxonomic identifier

192 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Rhodospirillaceae › Azospirillum

Protein attributes

Sequence length	469 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Sequence similarities	Belongs to the phosphohexose mutase family.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphomannomutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 469	469	Phosphomannomutase		PRO_0000147832
Sites
	Active site	106	1	Phosphoserine intermediate By similarity
	Metal binding	106	1	Magnesium; via phosphate group By similarity
	Metal binding	240	1	Magnesium By similarity
	Metal binding	242	1	Magnesium By similarity
	Metal binding	244	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	P45632 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 82A7D10244BD9FEF	FASTA	469	51,130
	10 20 30 40 50 60 MSEAHTFHPT VLREYDIRGI VGSTLTAADA RAVGRLRHRG RPAAVRKTVC VGYDGRLSSP 70 80 90 100 110 120 ELEAAMVDGL VACGLHVLRI GLGPTPMLYF ATRDREAAAG IMITGSHNPP DYNGIKMMLG 130 140 150 160 170 180 KGPVYGRQIL DIGAIASKAD YVSGEGSSEQ LDIKDAYVER LLRDDDGTRD LTIAWDAGNG 190 200 210 220 230 240 ASGEDPAPPD REVPGKHVLL FDEIDGNFPN HHPDPTVEKN LVDLKAAVAE HGCDIGIGFD 250 260 270 280 290 300 GDGDRIGAID HLGRVVWGDQ LVAIYAADVL KSHPGATIIA DVKASQTLFD EIARLGGNPL 310 320 330 340 350 360 MWKTGHSLLK AKMAETGSPL AGEMSGHIFF ADKWYGFDDA LYCAVRLIGL VSKLNQPLSE 370 380 390 400 410 420 LRDRLPDVVN TPETRFQVSE ERKFQVVQEV EGRSSRLMAE GADVNDIDGV RVKDADGWWL 430 440 450 460 LRASNTQDVL VARAESGTRR SWERLKGMVV AHWKPPASRP FLRGRRQLH

References

[1]	Petersen D.J., Vanderleyden J. Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 29145 / Sp7 / DSM 1690 / IMET 11303.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U20583 Genomic DNA. Translation: AAA63608.1.
3D structure databases
ProteinModelPortal	P45632.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.40.120.10. 3 hits.
InterPro	IPR005844. A-D-PHexomutase_a/b/a-I. IPR016055. A-D-PHexomutase_a/b/a-I/II/III. IPR005845. A-D-PHexomutase_a/b/a-II. IPR005846. A-D-PHexomutase_a/b/a-III. IPR005843. A-D-PHexomutase_C. IPR016066. A-D-PHexomutase_CS. IPR005841. Alpha-D-phosphohexomutase_SF. [Graphical view]
Pfam	PF02878. PGM_PMM_I. 1 hit. PF02879. PGM_PMM_II. 1 hit. PF02880. PGM_PMM_III. 1 hit. PF00408. PGM_PMM_IV. 1 hit. [Graphical view]
PRINTS	PR00509. PGMPMM.
SUPFAM	SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

EXOC_AZOBR

Accession

Primary (citable) accession number: P45632

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	February 1, 1996
Last modified:	March 6, 2013
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program