ID A0A3P9CXR2_9CICH Unreviewed; 401 AA.
AC A0A3P9CXR2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=N-acetylaspartylglutamate synthase {ECO:0000256|ARBA:ARBA00012938};
DE EC=6.3.2.41 {ECO:0000256|ARBA:ARBA00012938};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005027128.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005027128.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005027128.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000622};
CC -!- SIMILARITY: Belongs to the RimK family.
CC {ECO:0000256|ARBA:ARBA00007854}.
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DR RefSeq; XP_004554191.1; XM_004554134.3.
DR AlphaFoldDB; A0A3P9CXR2; -.
DR STRING; 106582.ENSMZEP00005027128; -.
DR Ensembl; ENSMZET00005027996.1; ENSMZEP00005027128.1; ENSMZEG00005020236.1.
DR GeneID; 101477475; -.
DR KEGG; mze:101477475; -.
DR CTD; 284716; -.
DR GeneTree; ENSGT00390000014577; -.
DR OrthoDB; 4026633at2759; -.
DR Proteomes; UP000265160; LG20.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX.
DR NCBIfam; TIGR00768; rimK_fam; 1.
DR PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B-RELATED; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR Pfam; PF08443; RimK; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000265160}.
FT DOMAIN 115..300
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 347..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 44140 MW; C234E537A207912A CRC64;
MCSRVWFLTD RRISQEYPQV QILRALKEHC ADEDVEFRYL LMDQIVLTIC EGQLGLRAEQ
ELVTSYPQVV MVRVPTPWVQ SDSDITVLRH LEKMGCRLIN RPQAILNCVN KFWTFQELAG
HGVPLPDTFS YGGHDNFRKM IDEAEPLGYP VVVKNARGHR GKAVFLARDK HHLTDLCHVI
RHDTPYLFQE YIKESHGRDV RVVLVGGRII GSMLRCSTDG RMQSNCSLGG VGMMCPLSEE
GKQLAIKVSN ILGMDVCGID LLQLNDGSFV VCEANANVGF IAFDQACGMD VAGIVADYVL
SMLPNRLTRK MSLLSVVSST SETSSEPEVC NVPSGGGSLP EAVCNMSVGS TSSESDPELA
EPSQSSPCQS TAPSLPDLPD LADPAYNFNT LLANEIKLLT E
//
