RIMKB_BOVIN
ID RIMKB_BOVIN Reviewed; 386 AA.
AC Q0VCE9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal spinal cord;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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; BC120203; AAI20204.1; -; mRNA.
DR RefSeq; NP_001069581.1; NM_001076113.2.
DR RefSeq; XP_005207126.1; XM_005207069.3.
DR RefSeq; XP_010803841.1; XM_010805539.2.
DR RefSeq; XP_015326757.1; XM_015471271.1.
DR RefSeq; XP_015326758.1; XM_015471272.1.
DR RefSeq; XP_015326759.1; XM_015471273.1.
DR RefSeq; XP_015326760.1; XM_015471274.1.
DR AlphaFoldDB; Q0VCE9; -.
DR SMR; Q0VCE9; -.
DR STRING; 9913.ENSBTAP00000004262; -.
DR PaxDb; Q0VCE9; -.
DR PRIDE; Q0VCE9; -.
DR Ensembl; ENSBTAT00000004262; ENSBTAP00000004262; ENSBTAG00000003291.
DR GeneID; 538579; -.
DR KEGG; bta:538579; -.
DR CTD; 57494; -.
DR VEuPathDB; HostDB:ENSBTAG00000003291; -.
DR VGNC; VGNC:33971; RIMKLB.
DR eggNOG; ENOG502QT4M; Eukaryota.
DR GeneTree; ENSGT00390000014577; -.
DR HOGENOM; CLU_054353_3_1_1; -.
DR InParanoid; Q0VCE9; -.
DR OMA; DAAYNFN; -.
DR OrthoDB; 753616at2759; -.
DR TreeFam; TF332035; -.
DR Reactome; R-BTA-8964539; Glutamate and glutamine metabolism.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000003291; Expressed in oviduct epithelium and 107 other tissues.
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..386
FT /note="Beta-citrylglutamate synthase B"
FT /id="PRO_0000282570"
FT DOMAIN 119..304
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT REGION 327..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 193..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 264
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 277
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 277
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 279
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ SEQUENCE 386 AA; 42550 MW; 6E4A2A43E068114D CRC64;
MCSSVAAKLW FLTDRRIRED YPQKEILRAL KAKCCEEELD FRAVVMDELV LTVEQGNLGL
RINGELITAY PQVVVVRVPT PWVQSDSDIT VLRHLEKMGC RLMNRPQAIL NCVNKFWTFQ
ELAGHGVPLP DTFSYGGHEN FAKMIDEAEV LEFPMVVKNT RGHRGKAVFL ARDKHHLADL
SHLIRHEAPY LFQKYVKESH GRDVRVIVVG GRVVGTMLRC STDGRMQSNC SLGGVGMMCS
LSEQGKQLAI QVSNILGMDV CGIDLLMKDD GSFCVCEANA NVGFIAFDKA CNLDVAGIIA
DYAASLLPSG RLTRRMSLLS VVSTASETSE PELGPQANTA VDNMSASSSS VDSDPETTER
ELLTKLPGGL FNMNQLLANE IKLLVE
