ID A0A139I1K7_9PEZI Unreviewed; 879 AA.
AC A0A139I1K7;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=N-acetyltransferase domain-containing protein {ECO:0000259|PROSITE:PS51731};
GN ORFNames=AC579_4459 {ECO:0000313|EMBL:KXT08610.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT08610.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT08610.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT08610.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) 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. {ECO:0000256|ARBA:ARBA00004862,
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|ARBA:ARBA00007239,
CC ECO:0000256|PIRNR:PIRNR036440}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the acetylglutamate
CC kinase family. {ECO:0000256|ARBA:ARBA00006830,
CC 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:KXT08610.1}.
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DR EMBL; LFZO01000423; KXT08610.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139I1K7; -.
DR STRING; 113226.A0A139I1K7; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000073492; 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: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:0070401; F:NADP+ binding; IEA:InterPro.
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 HAMAP; MF_00150; ArgC_type1; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR004662; AcgluKinase_fam.
DR InterPro; IPR023013; AGPR_AS.
DR InterPro; IPR000706; AGPR_type-1.
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 NCBIfam; TIGR01850; argC; 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 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|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR036440};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR036440};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|PIRNR:PIRNR036440};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268,
KW ECO:0000256|PIRNR:PIRNR036440};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR036440};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR036440};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR036440};
KW Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036440};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 334..488
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51731"
FT ACT_SITE 694
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 879 AA; 97140 MW; 0A6A5715CBD31A60 CRC64;
MQSLARPLCR QLARQRRCLA RQAFTVTTGP IARRQYASHR SDDKSARSAV ISVLNNIASK
REVQQYLAQF TSVSSQQFAV IKVGGAILTD YIDVLCASLR NLNQMGLYPV IIHGAGPQLN
RLLEEAGVEP KYNEGIRITD GKTLGVARKL FLQENLKLVE ALESWGVKAR PITSGVLMAD
YKDKDVYQFV GEVNQVNAGS IKAAIADGYI PVLTCMAESE EGQVLNVNAD KAAAELAKAL
VPLKIVYLSE KGGIYDKETG KLIEAINLDE EYEVYMKKPW VIHGTRSKIR DIKTLLDELP
RSSSVAIIHP ESLERELFTH SGAGTLIRRG TKLQQAENMK QFGDLAKLKQ TLVRDRAGLD
AAGVVDRYLE ILESRPFKAY YDDNMEALAI VLPPDNTPNA LAQLATFTIT RGAWLSNIAD
NVFQNVKRDF PKLAWTVKQD DENLTWFSEK ADGSIARGGE VLFWYGIDSP DEVRELMSEF
VKHGRKMFGD TNLESHIHRA NSTAQRIRAN AANLASNRRA FSTSTRPAAR VTTNGLQHVR
TYTTNPNPPL GIKNREKDYP SKVAIIGARG YTGQALIDLL NKHPNFDLCH VSSRELAGKE
LKGYDKKQII YENLSPEDIR KMAEKKAIDC WIMALPNGVC KPYVDAIEDS GHTDAVIVDL
SADYRFNSDW VYGLPELVQR SKIASATRIA NPGCYATAAQ LGIAPLVPYI PPFPAQPTVF
GVSGYSGAGT KPSPKNDVNV LTNNLIAYSL TDHIHEREIS AQLGTEIAFI PHVAVWFQGI
HHTISIPLAE KMASRDVRQL YQDRYDKEKL IKISGESPQV KNIAGKHGVE IGGFAVHSSG
KRVVINATID NLLKGAATQC LQNMNLALGY SEYEGIPLD
//
