ID A0A3A2ZYA8_9EURO Unreviewed; 887 AA.
AC A0A3A2ZYA8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Arginine-requiring protein 2 {ECO:0000256|ARBA:ARBA00030322};
GN ORFNames=PHISCL_01330 {ECO:0000313|EMBL:RJE26357.1};
OS Aspergillus sclerotialis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Polypaecilum.
OX NCBI_TaxID=2070753 {ECO:0000313|EMBL:RJE26357.1, ECO:0000313|Proteomes:UP000266188};
RN [1] {ECO:0000313|Proteomes:UP000266188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 366.77 {ECO:0000313|Proteomes:UP000266188};
RA Tafer H., Lopandic K.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 2/4. {ECO:0000256|ARBA:ARBA00004828,
CC ECO:0000256|PIRNR:PIRNR036440}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 3/4.
CC {ECO:0000256|PIRNR:PIRNR036440}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC ECO:0000256|PIRNR:PIRNR036440}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAGSA
CC dehydrogenase family. {ECO:0000256|PIRNR:PIRNR036440}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the acetylglutamate
CC kinase family. {ECO:0000256|PIRNR:PIRNR036440}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RJE26357.1}.
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DR EMBL; MVGC01000024; RJE26357.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A2ZYA8; -.
DR STRING; 2070753.A0A3A2ZYA8; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000266188; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04252; AAK_NAGK-fArgBP; 1.
DR CDD; cd04263; DUF619-NAGK-FABP; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR004662; AcgluKinase_fam.
DR InterPro; IPR023013; AGPR_AS.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR041734; NAGK-fArgBP.
DR InterPro; IPR011241; NAGK/NAGSA.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR006855; Vertebrate-like_GNAT_dom.
DR NCBIfam; TIGR00761; argB; 1.
DR PANTHER; PTHR23342; N-ACETYLGLUTAMATE SYNTHASE; 1.
DR PANTHER; PTHR23342:SF0; N-ACETYLGLUTAMATE SYNTHASE, MITOCHONDRIAL; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF04768; NAT; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR PIRSF; PIRSF036440; ARG5-6; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS01224; ARGC; 1.
DR PROSITE; PS51731; GNAT_NAGS; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR036440};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571,
KW ECO:0000256|PIRNR:PIRNR036440};
KW ATP-binding {ECO:0000256|PIRNR:PIRNR036440};
KW Kinase {ECO:0000256|PIRNR:PIRNR036440, ECO:0000313|EMBL:RJE26357.1};
KW Mitochondrion {ECO:0000256|PIRNR:PIRNR036440};
KW Multifunctional enzyme {ECO:0000256|PIRNR:PIRNR036440};
KW NADP {ECO:0000256|PIRNR:PIRNR036440};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR036440};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR036440};
KW Reference proteome {ECO:0000313|Proteomes:UP000266188};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036440};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 351..504
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51731"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 717
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 887 AA; 97225 MW; 524EE0B33C54933A CRC64;
MLSLRTAVRR ASTKPLRSLS APQTVSSVRL GSPVARHSLK ASAAPLLQSR RYSRAADPQL
SSTRSTVVQL LSNIGSKREV QQYLSHFTSV SSQQFAVIKV GGAIITEHLQ TLSSALAFLN
HVGLYPIVVH GAGPQLNRML EEAGVEPEFH DGIRVTDGKT LSLARKLFLE ENLKLVEELE
RMGVRARPLT AGVLFADYLD KEKYNLVGKI NGVNKKPIES AIEAGCLPIL TSMAETPDGQ
VLNVNADVAA GELARAVQPL KIVYLAEKGG LFNGDTGEKI SAINLDEEYD HLMNQWWVRH
GTRLKIKEMK ELLGDLPRSS SVAIIHPADL QKELFTDSGA GTLIRRGNKV HTKTSLSEFE
DLEKLKDVLV RDREGLDARA VVDRYVEGLK EANFKAYFDD PMEALAVVLP PQKGSSLAHL
ATLTITKSGW LTSVADNVFT NIRKDFPKLV WTVKEDDENL TWFFDKADGS LSREGEVLFW
YGIESGDEVK ELVLEFNKHG RQMFGDINLE SRLLRTAQAA SHIGKGFGTS GASVEQRRAF
SSSSNALRAA RSARPMVPVN VRTYATTNPN PPLGEKNMSN NRPSKVALIG ARGYTGQALI
NLLNAHPHMD LRHVSSRELA GKKLQGYDKR QITYENLSPE DVQRMAENGD VDCWVMALPN
GICKPFVDAV DKVSQKDNVI VDLSADYRFD SNWTYGLPEL VSRSTIAQAT RISNPGCYAT
AAQIGIAPLV PYLGGQPPSS VSPDTLAPAP SPARRTILTN HIHEKEISSQ LGTDVAFIPH
VAVWFQGIHH SISIPLKQEM TSRDIRNIFH DRYAGERLVQ VVGEAPLVKN IAGRHGVDVG
GFAVHTSGKR VVVCATIDNL LKGAATQCLQ NMNLALGYSE YEGIPLE
//
