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Q7UUZ2 (Q7UUZ2_RHOBA) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
[Protein-PII] uridylyltransferase HAMAP MF_00277
Short name=PII uridylyl-transferase HAMAP MF_00277
EC=2.7.7.59 HAMAP MF_00277
Alternative name(s):
UTase HAMAP MF_00277
Uridylyl-removing enzyme HAMAP MF_00277
Gene names
Name:glnD HAMAP MF_00277 EMBL CAD72935.1
Ordered Locus Names:RB2974
OrganismRhodopirellula baltica (strain SH1)
Taxonomic identifier243090 [NCBI]
Taxonomic lineageBacteria › Planctomycetes › Planctomycetacia › Planctomycetales › Planctomycetaceae › Rhodopirellula

Protein attributes

Sequence length883 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Adenylation and deadenylation of glutamate--ammonia ligase By similarity. SAAS SAAS005190

Modifies, by uridylylation or deuridylylation the PII (glnB) regulatory protein By similarity. HAMAP MF_00277 SAAS SAAS013546

Catalytic activity

ATP + [L-glutamate:ammonia ligase (ADP-forming)] = diphosphate + adenylyl-[L-glutamate:ammonia ligase (ADP-forming)]. SAAS SAAS005190

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII]. HAMAP MF_00277 SAAS SAAS013546

Sequence similarities

Belongs to the glnD family. HAMAP MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q7UUZ2 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: E16AAA4FCB626D53

FASTA883100,307
        10         20         30         40         50         60 
MASSGSLPSL ARQCRDRLND GRGRIESRFR AGLPSVQTAT ALTDLYDDVI EKIWQDSLER 

        70         80         90        100        110        120 
ASSSVKASQL SQLSLVAHGG YGRRDLSPYS DADLMLLTTR RSAAAAAQVA STFVRDITDA 

       130        140        150        160        170        180 
GIDCGFSVRT PRECCTLAWA DAKIYTSLTE SRLCFGNEQT FDRYFDRFRA GARRRRNYLN 

       190        200        210        220        230        240 
HQSLMARREE RHKWGETNYL LRPNVKRSRG GLRDIQLVRW LGFATHGATS LEQLNKLNAL 

       250        260        270        280        290        300 
SDEDYGTLRR AHAFMLRLRH ELHFRTKRAQ DVLDRPTQLD IAEDWGYQGR SGVLPVEDFM 

       310        320        330        340        350        360 
QDYFEHTRGV RYVAAYFHDD TRIRSRAAGA VESVMSRRID ENIRMGPTHI WVKSNTLEQF 

       370        380        390        400        410        420 
AQSLPDVLRL IQLANHHSRR IAHPTWQAIR KSMQDREATP PDQPAVDAFL ELLKDPGRLA 

       430        440        450        460        470        480 
SLLRRLHELR ILDQLIPAMG RCRGLLQFNA YHKYTVDAHC IRAVEAATDF IDAENAMGRR 

       490        500        510        520        530        540 
YRRLKDKGLL HLALLIHDLG KGYEEDHSEV GRRIAGDVAD LFHLSADDKD TLQWLIHKHL 

       550        560        570        580        590        600 
LVNEVAFRHD LNDPEVVHKF AAEVGSISRL ELLLIHTVAD LQAVGPDVLN DWKMGLIEDL 

       610        620        630        640        650        660 
YLRARRYFET GNLPGENEAD LDSKIEQVKE SLAEKKLDPS LIEFAKDMPL SLLRQHSTDD 

       670        680        690        700        710        720 
LIHEMHQVGE WLTHNPGCYC AGAVDPAASA VRYTIVLRQG ERRVGVFARI TAAFSACGLS 

       730        740        750        760        770        780 
IMRANVETVG EDLLWDQFWV NDPELKQRQP ESRIEEVCRV VTKALDDPDS VMPTPRRVWQ 

       790        800        810        820        830        840 
TQGAKEPSSV LLLPTKVLFD NDTFDHQTIL SMFTYDRPSL LSDISGTLSQ LDVVIQFAKI 

       850        860        870        880 
DTHLDQIADV FYVTNPDGSP ITDSDRQETI RNALVDAVRK PLP

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References

[1]"Complete genome sequence of the marine planctomycete Pirellula sp. strain 1."
Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., Reinhardt R.
Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003) [PubMed: 12835416] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX294138 Genomic DNA. Translation: CAD72935.1.
RefSeqNP_865251.1. NC_005027.1.

3D structure databases

ProteinModelPortalQ7UUZ2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1792122.
GenomeReviewsGene locus RB2974 in contig BX119912_GR.
KEGGrba:RB2974.
NMPDRfig|243090.1.peg.1591.
PATRIC23244169. VBIRhoBal59814_1370.

Phylogenomic databases

OMAMQHDLFH.
PhylomeDBQ7UUZ2.
ProtClustDBCLSK2758744.

Enzyme and pathway databases

BioCycPSP117:RB2974-MONOMER.

Family and domain databases

HAMAPMF_00277. PII_uridylyl_transf.
[Tree]
InterProIPR010043. GlnD_Uridyltrans.
IPR005190. GlnE_rpt_dom.
IPR023279. HD.
IPR003607. Metal-dep_PHydrolase_HD_dom.
IPR006674. Metal-dep_PHydrolase_HD_sub.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
Gene3DG3DSA:1.10.3210.10. HD. 1 hit.
KOK00990.
PANTHERPTHR13734:SF1. GlnD_Uridyltrans. 1 hit.
PfamPF08335. GlnD_UR_UTase. 1 hit.
PF03710. GlnE. 1 hit.
PF01966. HD. 1 hit.
[Graphical view]
PIRSFPIRSF006288. PII_uridyltransf. 1 hit.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsTIGR01693. UTase_glnD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ7UUZ2_RHOBA
AccessionPrimary (citable) accession number: Q7UUZ2
Entry history
Integrated into UniProtKB/TrEMBL: October 1, 2003
Last sequence update: October 1, 2003
Last modified: December 14, 2011
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info