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Protein

Beta-citrylglutamate synthase B

Gene

Rimklb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the synthesis of beta-citryl-L-glutamate and N-acetyl-L-aspartyl-L-glutamate. Beta-citryl-L-glutamate is synthesized more efficiently than N-acetyl-L-aspartyl-L-glutamate.2 Publications

Catalytic activityi

ATP + citrate + L-glutamate = ADP + phosphate + beta-citryl-L-glutamate.2 Publications
ATP + N-acetyl-L-aspartate + L-glutamate = ADP + phosphate + N-acetyl-L-aspartyl-L-glutamate.2 Publications

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium or manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei158 – 1581ATPBy similarity
Binding sitei219 – 2191ATPBy similarity
Metal bindingi264 – 2641Magnesium or manganese 1PROSITE-ProRule annotation
Metal bindingi277 – 2771Magnesium or manganese 1PROSITE-ProRule annotation
Metal bindingi277 – 2771Magnesium or manganese 2PROSITE-ProRule annotation
Metal bindingi279 – 2791Magnesium or manganese 2PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi193 – 20311ATPPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • citrate-L-glutamate ligase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • N-acetyl-L-aspartate-L-glutamate ligase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.3.1.17. 3474.
6.3.2.41. 3474.
6.3.2.B11. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-citrylglutamate synthase B (EC:6.3.1.172 Publications)
Alternative name(s):
N-acetyl-aspartylglutamate synthetase B (EC:6.3.2.411 Publication)
Short name:
NAAG synthetase B
Short name:
NAAGS
Ribosomal protein S6 modification-like protein B
Gene namesi
Name:Rimklb
Synonyms:Fam80b, Kiaa1238
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1918325. Rimklb.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 387387Beta-citrylglutamate synthase BPRO_0000282572Add
BLAST

Proteomic databases

MaxQBiQ80WS1.
PaxDbiQ80WS1.
PRIDEiQ80WS1.

Expressioni

Tissue specificityi

Strongly expressed in brain and testis. Expressed in eyes, thymus, lung, kidney, skeletal muscle, spleen, skin and heart. Expressed in neurons of the neocortex, the gray matter and Purkinje cells.1 Publication

Gene expression databases

BgeeiQ80WS1.
ExpressionAtlasiQ80WS1. baseline and differential.
GenevisibleiQ80WS1. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000064467.

Structurei

3D structure databases

ProteinModelPortaliQ80WS1.
SMRiQ80WS1. Positions 92-297.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini119 – 304186ATP-graspPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the RimK family.Curated
Contains 1 ATP-grasp domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IGDC. Eukaryota.
COG0189. LUCA.
GeneTreeiENSGT00390000014577.
HOGENOMiHOG000043112.
HOVERGENiHBG108408.
InParanoidiQ80WS1.
KOiK18310.
OMAiHFKVCEA.
OrthoDBiEOG7GBFWX.
PhylomeDBiQ80WS1.
TreeFamiTF332035.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013651. ATP-grasp_RimK-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR016185. PreATP-grasp_dom.
IPR004666. RpS6_RimK/Lys_biosynth_LsyX.
[Graphical view]
PfamiPF08443. RimK. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00768. rimK_fam. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q80WS1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MCSSVTGKLW FLTDRRIRED YPQKEILRAL KAKCCEEELD FRAVVMDEMV
60 70 80 90 100
LTVEQGNLGL RISGELISAY PQVVVVRVPT PWVQSDSDIT VLRHLEKMGC
110 120 130 140 150
RLMNRPQAIL NCVNKFWTFQ ELAGHGVPLP DTFSYGGHEN FAKMIDEAEV
160 170 180 190 200
LEFPMVVKNT RGHRGKAVFL ARDKHHLADL SHLIRHEAPY LFQKYIKESH
210 220 230 240 250
GRDVRVIVVG GRVVGTMLRC STDGRMQSNC SLGGVGMMCS LSEQGKQLAI
260 270 280 290 300
QVSNILGTDV CGIDLLMKDD GSFCVCEANA NVGFIAFDKA CNLDVAGIIA
310 320 330 340 350
DYAASLLPAG RLTRRMSLLS VVSTASETSE PELGPPASAA VDNMSASSSS
360 370 380
VDSDPESTTE REMLTKLPGG LFNMNQLLAN EIKLLVE
Length:387
Mass (Da):42,528
Last modified:June 1, 2003 - v1
Checksum:i97B90EABDD414CC6
GO
Isoform 2 (identifier: Q80WS1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: Missing.
     58-58: L → M

Note: No experimental confirmation available.
Show »
Length:330
Mass (Da):35,868
Checksum:i060349D872EBA2D9
GO
Isoform 3 (identifier: Q80WS1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: Missing.
     58-58: L → M
     282-308: VGFIAFDKACNLDVAGIIADYAASLLP → PFQEPKYTNTNKQKILRENTFLLPPSC
     309-387: Missing.

Note: No experimental confirmation available.
Show »
Length:251
Mass (Da):27,988
Checksum:iDB0DA44696FFCE3D
GO

Sequence cautioni

The sequence BAD32413.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5757Missing in isoform 2 and isoform 3. 1 PublicationVSP_024200Add
BLAST
Alternative sequencei58 – 581L → M in isoform 2 and isoform 3. 1 PublicationVSP_024201
Alternative sequencei282 – 30827VGFIA…ASLLP → PFQEPKYTNTNKQKILRENT FLLPPSC in isoform 3. 1 PublicationVSP_024202Add
BLAST
Alternative sequencei309 – 38779Missing in isoform 3. 1 PublicationVSP_024203Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK173135 mRNA. Translation: BAD32413.1. Different initiation.
AK016936 mRNA. Translation: BAB30506.1.
AK039398 mRNA. Translation: BAC30339.1.
BC052078 mRNA. Translation: AAH52078.1.
CCDSiCCDS39622.1. [Q80WS1-1]
RefSeqiNP_081940.1. NM_027664.1. [Q80WS1-1]
XP_011239417.1. XM_011241115.1. [Q80WS1-1]
XP_011239418.1. XM_011241116.1. [Q80WS1-1]
XP_011239419.1. XM_011241117.1. [Q80WS1-1]
XP_011239420.1. XM_011241118.1. [Q80WS1-1]
XP_011239421.1. XM_011241119.1. [Q80WS1-1]
XP_011239422.1. XM_011241120.1. [Q80WS1-2]
UniGeneiMm.277939.

Genome annotation databases

EnsembliENSMUST00000068242; ENSMUSP00000064467; ENSMUSG00000040649. [Q80WS1-1]
ENSMUST00000146274; ENSMUSP00000138104; ENSMUSG00000040649. [Q80WS1-3]
ENSMUST00000204731; ENSMUSP00000144770; ENSMUSG00000040649. [Q80WS1-2]
GeneIDi108653.
KEGGimmu:108653.
UCSCiuc009dpf.1. mouse. [Q80WS1-2]
uc009dpg.1. mouse. [Q80WS1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK173135 mRNA. Translation: BAD32413.1. Different initiation.
AK016936 mRNA. Translation: BAB30506.1.
AK039398 mRNA. Translation: BAC30339.1.
BC052078 mRNA. Translation: AAH52078.1.
CCDSiCCDS39622.1. [Q80WS1-1]
RefSeqiNP_081940.1. NM_027664.1. [Q80WS1-1]
XP_011239417.1. XM_011241115.1. [Q80WS1-1]
XP_011239418.1. XM_011241116.1. [Q80WS1-1]
XP_011239419.1. XM_011241117.1. [Q80WS1-1]
XP_011239420.1. XM_011241118.1. [Q80WS1-1]
XP_011239421.1. XM_011241119.1. [Q80WS1-1]
XP_011239422.1. XM_011241120.1. [Q80WS1-2]
UniGeneiMm.277939.

3D structure databases

ProteinModelPortaliQ80WS1.
SMRiQ80WS1. Positions 92-297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000064467.

Proteomic databases

MaxQBiQ80WS1.
PaxDbiQ80WS1.
PRIDEiQ80WS1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000068242; ENSMUSP00000064467; ENSMUSG00000040649. [Q80WS1-1]
ENSMUST00000146274; ENSMUSP00000138104; ENSMUSG00000040649. [Q80WS1-3]
ENSMUST00000204731; ENSMUSP00000144770; ENSMUSG00000040649. [Q80WS1-2]
GeneIDi108653.
KEGGimmu:108653.
UCSCiuc009dpf.1. mouse. [Q80WS1-2]
uc009dpg.1. mouse. [Q80WS1-1]

Organism-specific databases

CTDi57494.
MGIiMGI:1918325. Rimklb.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IGDC. Eukaryota.
COG0189. LUCA.
GeneTreeiENSGT00390000014577.
HOGENOMiHOG000043112.
HOVERGENiHBG108408.
InParanoidiQ80WS1.
KOiK18310.
OMAiHFKVCEA.
OrthoDBiEOG7GBFWX.
PhylomeDBiQ80WS1.
TreeFamiTF332035.

Enzyme and pathway databases

BRENDAi6.3.1.17. 3474.
6.3.2.41. 3474.
6.3.2.B11. 3474.

Miscellaneous databases

PROiQ80WS1.
SOURCEiSearch...

Gene expression databases

BgeeiQ80WS1.
ExpressionAtlasiQ80WS1. baseline and differential.
GenevisibleiQ80WS1. MM.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013651. ATP-grasp_RimK-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR016185. PreATP-grasp_dom.
IPR004666. RpS6_RimK/Lys_biosynth_LsyX.
[Graphical view]
PfamiPF08443. RimK. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00768. rimK_fam. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Fetal brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Spinal cord and Testis.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Brain.
  4. "Molecular characterization of N-acetylaspartylglutamate synthetase."
    Becker I., Lodder J., Gieselmann V., Eckhardt M.
    J. Biol. Chem. 285:29156-29164(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  5. "Molecular identification of N-acetylaspartylglutamate synthase and beta-citrylglutamate synthase."
    Collard F., Stroobant V., Lamosa P., Kapanda C.N., Lambert D.M., Muccioli G.G., Poupaert J.H., Opperdoes F., Van Schaftingen E.
    J. Biol. Chem. 285:29826-29833(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiRIMKB_MOUSE
AccessioniPrimary (citable) accession number: Q80WS1
Secondary accession number(s): Q69ZN3, Q8CA77, Q9D3Z1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: June 1, 2003
Last modified: June 8, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

N-acetyl-L-aspartyl-L-glutamate (NAAG) is the most abundant dipeptide present in vertebrate central nervous system (CNS). Beta-citryl-L-glutamate, a structural analog of NAAG, is present in testis and immature brain.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.