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Q5P9T3

- PANC_ANAMM

UniProt

Q5P9T3 - PANC_ANAMM

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Protein

Pantothenate synthetase

Gene

panC

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.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 donorUniRule annotation
Binding sitei59 – 591Beta-alanineUniRule annotation
Binding sitei59 – 591PantoateUniRule annotation
Binding sitei174 – 1741ATP; via amide nitrogen and carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi28 – 358ATPUniRule annotation
Nucleotide bindingi145 – 1484ATPUniRule annotation
Nucleotide bindingi182 – 1854ATPUniRule annotation

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 synthetaseUniRule annotation (EC:6.3.2.1UniRule annotation)
Short name:
PSUniRule annotation
Alternative name(s):
Pantoate--beta-alanine ligaseUniRule annotation
Pantoate-activating enzymeUniRule annotation
Gene namesi
Name:panCUniRule annotation
Ordered Locus Names:AM1089
OrganismiAnaplasma marginale (strain St. Maries)
Taxonomic identifieri234826 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma
ProteomesiUP000006557: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 277277Pantothenate synthetasePRO_0000305391Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi234826.AM1089.

Structurei

3D structure databases

ProteinModelPortaliQ5P9T3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pantothenate synthetase family.UniRule annotation

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

« Hide

        10         20         30         40         50
MEIVRDVESV RAVLRPFTNR KIGLVPTMGA LHSGHLSLVH EMKKHADVVI
60 70 80 90 100
VSIFVNPLQF SPGEDYEKYP RCEEVDCEKC ASAGVDVVYI PSAEGMYPDG
110 120 130 140 150
FSTSVDIGPM ARELCGASRQ NFINGIMVVL IKLVMQTNAH CMILGEKDYQ
160 170 180 190 200
MLHLTRQLFR DLNIGVDVLQ GNTVRSAEGL ALSSRHQYLS SAEITKANFL
210 220 230 240 250
YGFLLEVGQQ LSDDPHGQQE IIARGKLRLE QEGFEVDYLE VRDNNTLEHM
260 270
QTFRKPARVF LAVYLGNCRL IDNVLLA
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. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: October 29, 2014
This is version 60 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.UniRule annotation

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