ID A0A2D0R0B7_ICTPU Unreviewed; 397 AA.
AC A0A2D0R0B7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=N-acetylaspartylglutamate synthase {ECO:0000256|ARBA:ARBA00012938};
DE EC=6.3.2.41 {ECO:0000256|ARBA:ARBA00012938};
GN Name=rimkla {ECO:0000313|RefSeq:XP_017324088.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017324088.1};
RN [1] {ECO:0000313|RefSeq:XP_017324088.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017324088.1};
RG RefSeq;
RL Submitted (NOV-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_017324088.1; XM_017468599.3.
DR AlphaFoldDB; A0A2D0R0B7; -.
DR STRING; 7998.ENSIPUP00000001455; -.
DR Ensembl; ENSIPUT00000001528; ENSIPUP00000001455; ENSIPUG00000001046.
DR GeneID; 108265850; -.
DR KEGG; ipu:108265850; -.
DR CTD; 284716; -.
DR OMA; FNEMEDA; -.
DR OrthoDB; 4026633at2759; -.
DR Proteomes; UP000221080; Chromosome 5.
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}.
FT DOMAIN 115..300
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 350..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 397 AA; 43552 MW; C2B07D8D3F2DA693 CRC64;
MCSRVWFVTD RRISQEYPQV QILRALKERC SEDDVDFRYL LMDEIVITIM DGQLGLRVGQ
EVVTSYPQVA VVRVPTPWVQ SDSDITVLRH LEKMGCRLVN RPQAILNCVN KFWTFQELAG
HGVPLPDTYS YGGHDNFRKM IDEAEPLGYP VVVKNARGHR GKAVFLARDK HHLSDLCHLI
RHDAPYLFQE YVKESHGRDV RVVLVGGRVI GSMLRCSTDG RMQSNCSLGG VGVMCPLSEQ
GKQLAVQVSN ILGMDVCGID LLQLNEGSFV VCEANANVGF IAFDQACGMD VAGIVADYAL
SLLPSRLSRK MSLLSVVSSA SETSSEPEVC IPPEVCAPVP PCAIPDAIPD GVSTMSTSST
SSESEAELAE MSHPQSVPDP AYNINSILAK EIKLLTE
//