RIMKB_DANRE
ID RIMKB_DANRE Reviewed; 405 AA.
AC Q66HZ2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Beta-citrylglutamate synthase B;
DE EC=6.3.1.17 {ECO:0000250|UniProtKB:Q80WS1};
DE AltName: Full=N-acetyl-aspartylglutamate synthetase B;
DE Short=NAAG synthetase B;
DE Short=NAAGS;
DE EC=6.3.2.41 {ECO:0000250|UniProtKB:Q80WS1};
DE AltName: Full=Ribosomal protein S6 modification-like protein B;
GN Name=rimklb; Synonyms=fam80b; ORFNames=zgc:92164;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of beta-citryl-L-glutamate and N-
CC acetyl-L-aspartyl-L-glutamate. Beta-citryl-L-glutamate is synthesized
CC more efficiently than N-acetyl-L-aspartyl-L-glutamate.
CC {ECO:0000250|UniProtKB:Q80WS1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + citrate + L-glutamate = ADP + beta-citrylglutamate +
CC H(+) + phosphate; Xref=Rhea:RHEA:40043, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16947, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:76942, ChEBI:CHEBI:456216;
CC EC=6.3.1.17; Evidence={ECO:0000250|UniProtKB:Q80WS1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + N-acetyl-L-aspartate = ADP + H(+) + N-
CC acetyl-L-aspartyl-L-glutamate + phosphate; Xref=Rhea:RHEA:40035,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16953, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:76931,
CC ChEBI:CHEBI:456216; EC=6.3.2.41;
CC Evidence={ECO:0000250|UniProtKB:Q80WS1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: N-acetyl-L-aspartyl-L-glutamate (NAAG) is the most
CC abundant dipeptide present in vertebrate central nervous system (CNS).
CC Beta-citryl-L-glutamate, a structural analog of NAAG, is present in
CC testis and immature brain. {ECO:0000250|UniProtKB:Q80WS1}.
CC -!- SIMILARITY: Belongs to the RimK family. {ECO:0000305}.
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DR EMBL; BC081615; AAH81615.1; -; mRNA.
DR RefSeq; NP_001004554.1; NM_001004554.2.
DR AlphaFoldDB; Q66HZ2; -.
DR SMR; Q66HZ2; -.
DR STRING; 7955.ENSDARP00000007712; -.
DR PaxDb; Q66HZ2; -.
DR Ensembl; ENSDART00000005337; ENSDARP00000007712; ENSDARG00000016830.
DR Ensembl; ENSDART00000189633; ENSDARP00000154796; ENSDARG00000112193.
DR GeneID; 447815; -.
DR KEGG; dre:447815; -.
DR CTD; 284716; -.
DR ZFIN; ZDB-GENE-040912-20; rimkla.
DR eggNOG; ENOG502QT4M; Eukaryota.
DR GeneTree; ENSGT00390000014577; -.
DR HOGENOM; CLU_054353_3_1_1; -.
DR InParanoid; Q66HZ2; -.
DR OrthoDB; 753616at2759; -.
DR PhylomeDB; Q66HZ2; -.
DR TreeFam; TF332035; -.
DR Reactome; R-DRE-8964539; Glutamate and glutamine metabolism.
DR PRO; PR:Q66HZ2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 8.
DR Bgee; ENSDARG00000016830; Expressed in blastula and 32 other tissues.
DR ExpressionAtlas; Q66HZ2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0072591; F:citrate-L-glutamate ligase activity; ISS:UniProtKB.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0072590; F:N-acetyl-L-aspartate-L-glutamate ligase activity; ISS:UniProtKB.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR004666; RpS6_RimK/Lys_biosynth_LsyX.
DR Pfam; PF08443; RimK; 1.
DR TIGRFAMs; TIGR00768; rimK_fam; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..405
FT /note="Beta-citrylglutamate synthase B"
FT /id="PRO_0000282573"
FT DOMAIN 115..300
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT REGION 359..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 189..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 260
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 273
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 273
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 275
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ SEQUENCE 405 AA; 44500 MW; 1AEBA9584788AEAA CRC64;
MCSRVWFITD RRISQEYPQI QILRALKERC VEDDVEFRYL LMDEIVLTIT DGQLGLRVGQ
EIVTSYPQVA VVRVPTPWVQ SDSDITVLRH LEKMGCRLVN RPQAILNCVN KFWTFQELAG
HGVPLPDTYS YGGHDNFRKM IDEAEPLGYP VVVKNARGHR GKAVFLARDK HHLSDLCHLI
RHEAPYLFQE YVKESHGRDV RVVLVGGRVI GSMLRCSTDG RMQSNCSLGG VGMMCPLSEQ
GKQLAVQVCN ILGMDVCGID LLQKNDGSFV VCEANANVGF IAFDQACGMD VAGIVADFVL
SLLPSRLSRK MSLLSVVSST SETSSEPEVC IPTEVIIPSE VCIPNEICPL GTTCPIPDAM
STMSTSSTSS ESEADLTETG PTPVGANPAY NINSLLASEM KLLTE
