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Q5NL15

- PANC_ZYMMO

UniProt

Q5NL15 - PANC_ZYMMO

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Protein

Pantothenate synthetase

Gene

panC

Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
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 sitei37 – 371Proton donorUniRule annotation
Binding sitei61 – 611Beta-alanineUniRule annotation
Binding sitei61 – 611PantoateUniRule annotation
Binding sitei153 – 1531PantoateUniRule annotation
Binding sitei176 – 1761ATP; via amide nitrogen and carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 378ATPUniRule annotation
Nucleotide bindingi147 – 1504ATPUniRule annotation
Nucleotide bindingi184 – 1874ATPUniRule 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:ZMO1954
OrganismiZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Taxonomic identifieri264203 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas
ProteomesiUP000001173: 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 – 287287Pantothenate synthetasePRO_0000305583Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi264203.ZMO1971.

Structurei

3D structure databases

ProteinModelPortaliQ5NL15.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pantothenate synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0414.
HOGENOMiHOG000175517.
OMAiASSKENH.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00158. PanC.
InterProiIPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamiPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00018. panC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5NL15-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLVIHTIAEL RAHLDEHRQN RRKIGLVPTM GFLHQGHMAL AQKAREESDV
60 70 80 90 100
VVLSIFVNPI QFGVNEDLDV YPRDLPHDIA LCKENGVDII FAPSVAEIYP
110 120 130 140 150
EPIMTSVEVQ SLSNILIGRH RPNHFRGVTT IVAKLLNIVE PDKIIFGEKD
160 170 180 190 200
YQQLIIVRRM IRDLSYKAEV IGVPIVREKD GLACSSRNAR LTKEDRAAAV
210 220 230 240 250
ILSQSLKKAQ KRILEGEKDV STIRQLIEDD IKSEARAKIQ SIDICHATKL
260 270 280
DTLDRIDNQP IVILLAVAFG DVVLIDQQLV TPKEKAL
Length:287
Mass (Da):32,260
Last modified:October 2, 2007 - v2
Checksum:i512DD8794CD529DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008692 Genomic DNA. Translation: AAV90578.2.
RefSeqiYP_163689.2. NC_006526.2.

Genome annotation databases

EnsemblBacteriaiAAV90578; AAV90578; ZMO1954.
GeneIDi3189355.
KEGGizmo:ZMO1954.
PATRICi32569246. VBIZymMob102260_1881.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008692 Genomic DNA. Translation: AAV90578.2 .
RefSeqi YP_163689.2. NC_006526.2.

3D structure databases

ProteinModelPortali Q5NL15.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 264203.ZMO1971.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAV90578 ; AAV90578 ; ZMO1954 .
GeneIDi 3189355.
KEGGi zmo:ZMO1954.
PATRICi 32569246. VBIZymMob102260_1881.

Phylogenomic databases

eggNOGi COG0414.
HOGENOMi HOG000175517.
OMAi ASSKENH.

Enzyme and pathway databases

UniPathwayi UPA00028 ; UER00005 .

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
HAMAPi MF_00158. PanC.
InterProi 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 TIGR00018. panC. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 31821 / ZM4 / CP4.
  2. Cited for: SEQUENCE REVISION.

Entry informationi

Entry nameiPANC_ZYMMO
AccessioniPrimary (citable) accession number: Q5NL15
Secondary accession number(s): Q5NL32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: October 29, 2014
This is version 66 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, Reference proteome

Documents

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

External Data

Dasty 3