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P44458

- CITXG_HAEIN

UniProt

P44458 - CITXG_HAEIN

Protein

Protein CitXG

Gene

citXG

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 2 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Bifunctional enzyme that catalyzes formation of 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A, and then the transfer of this prosthetic group precursor to the apo-acyl carrier protein (gamma chain) of the citrate lyase to yield the holo-acyl carrier protein.By similarity

    Catalytic activityi

    2'-(5-triphosphoribosyl)-3'-dephospho-CoA + citrate lyase apo-[acyl-carrier-protein] = citrate lyase holo-[acyl-carrier-protein] + diphosphate.
    ATP + 3'-dephospho-CoA = 2'-(5-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + adenine.

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. holo-citrate lyase synthase activity Source: UniProtKB-EC
    3. triphosphoribosyl-dephospho-CoA synthase activity Source: InterPro

    GO - Biological processi

    1. phosphorylation Source: InterPro
    2. prosthetic group biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein CitXG
    Including the following 2 domains:
    Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase (EC:2.7.7.61)
    Alternative name(s):
    Apo-ACP nucleodityltransferase
    Holo-ACP synthase
    Holo-citrate lyase synthase
    2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase (EC:2.4.2.52)
    Short name:
    2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthase
    Gene namesi
    Name:citXG
    Synonyms:citG
    Ordered Locus Names:HI_0021
    OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
    Taxonomic identifieri71421 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
    ProteomesiUP000000579: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 465465Protein CitXGPRO_0000214682Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi71421.HI0021.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 182182Apo-citrate lyase phosphoribosyl-dephospho-CoA transferaseAdd
    BLAST
    Regioni183 – 4652832-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthaseAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the CitX family.Curated
    In the C-terminal section; belongs to the CitG/MdcB family.Curated

    Phylogenomic databases

    eggNOGiCOG1767.
    KOiK13927.
    OMAiLAQNHDF.
    OrthoDBiEOG6WHNRS.

    Family and domain databases

    HAMAPiMF_00397. CitG.
    MF_00398. CitX.
    InterProiIPR002736. CitG.
    IPR005551. CitX.
    IPR017551. TriPribosyl-deP-CoA_syn_CitG.
    [Graphical view]
    PfamiPF01874. CitG. 1 hit.
    PF03802. CitX. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR03125. citrate_citG. 1 hit.
    TIGR03124. citrate_citX. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P44458-1 [UniParc]FASTAAdd to Basket

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    MQHFFTTFST EGSKISLEAL LNAREERAIL QQQLITQYGQ TLLCITLTAM    50
    GGVKKNALLD YVFTKALENL TALFTQLNIT AVKEIIRPLE TGHEAYFVLP 100
    IDARTLKVLM IELEESIPLA RLWDLDVFNA KGNLLSRTDF DLSPRTCLVC 150
    GENAKICART HKHEIDEIVD KIQSLAQNHD FAEHIGEQVY LALIQEARLS 200
    PKPGLVDAIN NGSHKDMNLH TFEQSAISLK PFFTQFVLKG MMTAHLSENQ 250
    ILSEIRPLGL LAEKAMFKVT DGVNTHKGAI FSFGLVCTAI GRLLAQKSLV 300
    QSAVDFDVKL ICSLVAQFTQ GLTDELKNYP EHLPSTAGVR LFQKYGLTGV 350
    RGEAENGFNL IQTLLPQFDE YHQLEWEHRL LILLLNLMAI NSDTNVVHRG 400
    GLAGLYFIQQ TAQDLLTDQH LVTDKTALTQ ALMKFDTACI ERNLSSGGSA 450
    DLLALTIFFL SFRGN 465
    Length:465
    Mass (Da):51,835
    Last modified:June 1, 2001 - v2
    Checksum:i4467221C3DB58A96
    GO

    Sequence cautioni

    The sequence AAC21699.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42023 Genomic DNA. Translation: AAC21699.1. Different initiation.
    PIRiE64140.
    RefSeqiNP_438194.1. NC_000907.1.

    Genome annotation databases

    EnsemblBacteriaiAAC21699; AAC21699; HI_0021.
    GeneIDi950919.
    KEGGihin:HI0021.
    PATRICi20188493. VBIHaeInf48452_0021.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L42023 Genomic DNA. Translation: AAC21699.1 . Different initiation.
    PIRi E64140.
    RefSeqi NP_438194.1. NC_000907.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 71421.HI0021.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC21699 ; AAC21699 ; HI_0021 .
    GeneIDi 950919.
    KEGGi hin:HI0021.
    PATRICi 20188493. VBIHaeInf48452_0021.

    Phylogenomic databases

    eggNOGi COG1767.
    KOi K13927.
    OMAi LAQNHDF.
    OrthoDBi EOG6WHNRS.

    Family and domain databases

    HAMAPi MF_00397. CitG.
    MF_00398. CitX.
    InterProi IPR002736. CitG.
    IPR005551. CitX.
    IPR017551. TriPribosyl-deP-CoA_syn_CitG.
    [Graphical view ]
    Pfami PF01874. CitG. 1 hit.
    PF03802. CitX. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR03125. citrate_citG. 1 hit.
    TIGR03124. citrate_citX. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

    Entry informationi

    Entry nameiCITXG_HAEIN
    AccessioniPrimary (citable) accession number: P44458
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 91 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Haemophilus influenzae
      Haemophilus influenzae (strain Rd): entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3