C1HPL9 (C1HPL9_9ESCH) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
L-arabinose isomerase HAMAP MF_00519
EC=5.3.1.4 HAMAP MF_00519

Gene names

Name:	araA HAMAP MF_00519
ORF Names:	ESAG_04090 EMBL EEH88378.1

Organism

Escherichia sp. 3_2_53FAA EMBL EEH88378.1

Taxonomic identifier

469598 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	500 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the conversion of L-arabinose to L-ribulose By similarity. HAMAP MF_00519 SAAS SAAS003762
Catalytic activity	L-arabinose = L-ribulose. HAMAP MF_00519 SAAS SAAS003762
Cofactor	Binds 1 manganese ion per subunit By similarity. HAMAP MF_00519 SAAS SAAS003762
Pathway	Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 1/3. HAMAP MF_00519 SAAS SAAS003762
Subunit structure	Homohexamer By similarity. HAMAP MF_00519
Sequence similarities	Belongs to the arabinose isomerase family. HAMAP MF_00519

Ontologies

Keywords
Biological process	Arabinose catabolism HAMAP MF_00519 SAAS SAAS003762 Carbohydrate metabolism
Ligand	Manganese HAMAP MF_00519 SAAS SAAS003762 Metal-binding HAMAP MF_00519 SAAS SAAS003762
Molecular function	Isomerase HAMAP MF_00519 SAAS SAAS003762 EMBL EEH88378.1
Gene Ontology (GO)
Biological process	arabinose catabolic process Inferred from electronic annotation. Source: HAMAP fucose metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	L-arabinose isomerase activity Inferred from electronic annotation. Source: HAMAP L-fucose isomerase activity Inferred from electronic annotation. Source: InterPro manganese ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Metal binding	306	1	Manganese By similarity HAMAP MF_00519
	Metal binding	333	1	Manganese By similarity HAMAP MF_00519
	Metal binding	350	1	Manganese By similarity HAMAP MF_00519
	Metal binding	450	1	Manganese By similarity HAMAP MF_00519

Sequences

	Sequence		Length	Mass (Da)
	C1HPL9 [UniParc]. Last modified May 26, 2009. Version 1. Checksum: E1B1B9F2FACF1FBD	FASTA	500	56,103
	10 20 30 40 50 60 MTIFDNYEVW FVIGSQHLYG PETLRQVTQH AEHVVNALNT EAKLPCKLVL KPLGTTPDEI 70 80 90 100 110 120 TAICRDANYD DRCAGLVVWL HTFSPAKMWI NGLTMLNKPL LQFHTQFNAA LPWDSIDMDF 130 140 150 160 170 180 MNLNQTAHGG REFGFIGARM RQQHAVVTGH WQDKQAHERI GSWMRQAVSK QDTRHLKVCR 190 200 210 220 230 240 FGDNMREVAV TDGDKVAAQI KFGFSVNTWA VGDLVQVVNS ISDGDVNALV DEYESCYTMT 250 260 270 280 290 300 PATQIHGEKR QNVLEAARIE LGMKRFLEQG GFHAFTTTFE DLHGLKQLPG LAVQRLMQQG 310 320 330 340 350 360 YGFAGEGDWK TAALLRIMKV MSTGLQGGTS FMEDYTYHFE KGNDLVLGSH MLEVCPSIAV 370 380 390 400 410 420 EEKPILDVQH LGIGGKDDPA RLIFNTQTGP AIVASLIDLG DRYRLLVNCI DTVKTPHSLP 430 440 450 460 470 480 KLPVANALWK AQPDLPTASE AWILAGGAHH TVFSHALNLN DMRQFAEMHD IEITVIDNDT 490 500 RLPAFKDALR WNEVYYGFRR

References

[1]

"The Genome Sequence of Escherichia sp. strain 3_2_53FAA." The Broad Institute Genome Sequencing Platform Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C. , Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Ambrose C., Lander E., Nusbaum C., Ilzarbe M., Galagan J., Birren B. Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: 3_2_53FAA EMBL EEH88378.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS999463 Genomic DNA. Translation: EEH88378.1.
3D structure databases
ProteinModelPortal	C1HPL9.
SMR	C1HPL9. Positions 1-498.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
PATRIC	29416852. VBIEscSp50726_3847.
Family and domain databases
HAMAP	MF_00519. Arabinose_Isome. [Tree]
InterPro	IPR024664. Ara_Isoase_C. IPR004216. Fuc/Ara_isomerase_C. IPR009015. Fucose_isomerase_N/cen. IPR003762. Lara_isomerase. [Graphical view]
Pfam	PF11762. Arabinose_Iso_C. 1 hit. PF02610. Arabinose_Isome. 1 hit. [Graphical view]
PIRSF	PIRSF001478. L-ara_isomerase. 1 hit.
ProDom	PD018364. Lara_isomerase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SUPFAM	SSF50443. Fuc_isomerase_C. 1 hit. SSF53743. Fuc_isomerase_N. 1 hit.
ProtoNet	Search...

Entry information

Entry name

C1HPL9_9ESCH

Accession

Primary (citable) accession number: C1HPL9

Entry history

Integrated into UniProtKB/TrEMBL:	May 26, 2009
Last sequence update:	May 26, 2009
Last modified:	December 14, 2011
This is version 14 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)