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P51035

- CISY_BARVB

UniProt

P51035 - CISY_BARVB

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Protein

Citrate synthase

Gene
gltA
Organism
Bartonella vinsonii subsp. berkhofii
Status
Reviewed - Annotation score: 2 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei39 – 391 By similarity
Active sitei97 – 971 By similarity

GO - Molecular functioni

  1. transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer Source: InterPro

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase (EC:2.3.3.16)
Gene namesi
Name:gltA
OrganismiBartonella vinsonii subsp. berkhofii
Taxonomic identifieri40933 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›112›112Citrate synthasePRO_0000169937Add
BLAST

Proteomic databases

PRIDEiP51035.

Structurei

3D structure databases

ProteinModelPortaliP51035.
SMRiP51035. Positions 1-111.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
InterProiIPR016143. Citrate_synth-like_sm_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P51035-1 [UniParc]FASTAAdd to Basket

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ANEACLKMLL EIGSVKRIPE FIARAKDKND PFRLMGFGHR VYKNYDPRAK    50
IMQKTCHEVL KELNIQNDPL LDIAIELEKI ALNDEYFVEK KLYPNVDFYS 100
GITLKALGFP TE 112
Length:112
Mass (Da):12,961
Last modified:October 1, 1996 - v1
Checksum:iA2A8CD9235629F7D
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei112 – 1121

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U28075 Genomic DNA. Translation: AAA74980.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U28075 Genomic DNA. Translation: AAA74980.1 .

3D structure databases

ProteinModelPortali P51035.
SMRi P51035. Positions 1-111.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P51035.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00717 .

Family and domain databases

Gene3Di 1.10.230.10. 1 hit.
InterProi IPR016143. Citrate_synth-like_sm_a-sub.
IPR002020. Citrate_synthase-like.
IPR016141. Citrate_synthase-like_core.
IPR019810. Citrate_synthase_AS.
[Graphical view ]
PANTHERi PTHR11739. PTHR11739. 1 hit.
Pfami PF00285. Citrate_synt. 1 hit.
[Graphical view ]
PRINTSi PR00143. CITRTSNTHASE.
SUPFAMi SSF48256. SSF48256. 1 hit.
PROSITEi PS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Jones D.C., Regnery R., Bowen M.
    Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiCISY_BARVB
AccessioniPrimary (citable) accession number: P51035
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Citrate synthase is found in nearly all cells capable of oxidative metabolism.

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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