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Q5P9T3

- PANC_ANAMM

UniProt

Q5P9T3 - PANC_ANAMM

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Protein

Pantothenate synthetase

Gene
panC, AM1089
Organism
Anaplasma marginale (strain St. Maries)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate By similarity.UniRule annotation

Catalytic activityi

ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei35 – 351Proton donor By similarity
Binding sitei59 – 591Beta-alanine By similarity
Binding sitei59 – 591Pantoate By similarity
Binding sitei174 – 1741ATP; via amide nitrogen and carbonyl oxygen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi28 – 358ATP By similarity
Nucleotide bindingi145 – 1484ATP By similarity
Nucleotide bindingi182 – 1854ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. pantoate-beta-alanine ligase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. pantothenate biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00028; UER00005.

Names & Taxonomyi

Protein namesi
Recommended name:
Pantothenate synthetase (EC:6.3.2.1)
Short name:
PS
Alternative name(s):
Pantoate--beta-alanine ligase
Pantoate-activating enzyme
Gene namesi
Name:panC
Ordered Locus Names:AM1089
OrganismiAnaplasma marginale (strain St. Maries)
Taxonomic identifieri234826 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma
ProteomesiUP000006557: Chromosome

Subcellular locationi

Cytoplasm Reviewed prediction UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 277277Pantothenate synthetaseUniRule annotationPRO_0000305391Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi234826.AM1089.

Structurei

3D structure databases

ProteinModelPortaliQ5P9T3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0414.
HOGENOMiHOG000175516.
KOiK01918.
OMAiEIDYVEV.
OrthoDBiEOG6Z6FZ4.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00158. PanC.
InterProiIPR004821. Cyt_trans-like.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamiPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5P9T3-1 [UniParc]FASTAAdd to Basket

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MEIVRDVESV RAVLRPFTNR KIGLVPTMGA LHSGHLSLVH EMKKHADVVI    50
VSIFVNPLQF SPGEDYEKYP RCEEVDCEKC ASAGVDVVYI PSAEGMYPDG 100
FSTSVDIGPM ARELCGASRQ NFINGIMVVL IKLVMQTNAH CMILGEKDYQ 150
MLHLTRQLFR DLNIGVDVLQ GNTVRSAEGL ALSSRHQYLS SAEITKANFL 200
YGFLLEVGQQ LSDDPHGQQE IIARGKLRLE QEGFEVDYLE VRDNNTLEHM 250
QTFRKPARVF LAVYLGNCRL IDNVLLA 277
Length:277
Mass (Da):31,057
Last modified:October 2, 2007 - v2
Checksum:i29ADC2883893FD5E
GO

Sequence cautioni

The sequence AAV86947.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000030 Genomic DNA. Translation: AAV86947.1. Different initiation.
RefSeqiYP_154202.1. NC_004842.2.

Genome annotation databases

EnsemblBacteriaiAAV86947; AAV86947; AM1089.
GeneIDi3171235.
KEGGiama:AM1089.
PATRICi20948069. VBIAnaMar46146_0947.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000030 Genomic DNA. Translation: AAV86947.1 . Different initiation.
RefSeqi YP_154202.1. NC_004842.2.

3D structure databases

ProteinModelPortali Q5P9T3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 234826.AM1089.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAV86947 ; AAV86947 ; AM1089 .
GeneIDi 3171235.
KEGGi ama:AM1089.
PATRICi 20948069. VBIAnaMar46146_0947.

Phylogenomic databases

eggNOGi COG0414.
HOGENOMi HOG000175516.
KOi K01918.
OMAi EIDYVEV.
OrthoDBi EOG6Z6FZ4.

Enzyme and pathway databases

UniPathwayi UPA00028 ; UER00005 .

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
HAMAPi MF_00158. PanC.
InterProi IPR004821. Cyt_trans-like.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view ]
PANTHERi PTHR21299:SF1. PTHR21299:SF1. 1 hit.
Pfami PF02569. Pantoate_ligase. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
    Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: St. Maries.

Entry informationi

Entry nameiPANC_ANAMM
AccessioniPrimary (citable) accession number: Q5P9T3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: May 14, 2014
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity.

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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