ID A0A0P7B4C2_9HYPO Unreviewed; 882 AA.
AC A0A0P7B4C2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Protein arg-6, mitochondrial {ECO:0000313|EMBL:KPM36497.1};
GN ORFNames=AK830_g10069 {ECO:0000313|EMBL:KPM36497.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM36497.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM36497.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM36497.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-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:KPM36497.1}.
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DR EMBL; LKCW01000201; KPM36497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7B4C2; -.
DR STRING; 78410.A0A0P7B4C2; -.
DR OrthoDB; 987250at2759; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000050424; 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:0046983; F:protein dimerization activity; 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; IPR012280; Semialdhyde_DH_dimer_dom.
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 Pfam; PF02774; Semialdhyde_dhC; 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:UP000050424};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036440};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 341..494
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51731"
FT REGION 539..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 700
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 882 AA; 96256 MW; 66BEBC6E5370103A CRC64;
MLSATAVAFR AGARRAAPRA AARAGAVSAQ IRCPNASRAL STSRALASPP ARDRTREIVA
QAVSSIGSKR EGQQYLKLFT SVSSKKFAVI KVGGAILTEY LDELCRSLLF LNELGLYPVI
VHGAGPQLNR LLEEAGVEPQ FEEGIRVTDA KTLGIARKLF LEENLKLVDR LDQLGVATRS
ISGAFMADYL DKDKWQYVGK ITKVNKQAIE NSIDAGYIPI LTSMAESDDG RLLNVNADVA
AAELARALEP LKVVYLSEKG GLFDGEGEHI SHINLDAEFD HLMAQPWCRY GTRLKIKEIK
ELLDTLPRTS SVAIIHPSDL QKELFTDSGA GTLIRRGDKV QKVSAVEDFK DLEKLKATLI
RGREGMDAEA TVDHFINFLK ANSFTAYYDD ALQCLAVVLP AGGERSVATL ATLNITKAGW
LSNIAENVFD AIKKEHPSLI WTVSEEDENL TWFFDKADGS FNKNGSVLFY YGCDLRSDAL
IPAYEHFIEH GRTMLGDTNL ESRLRSAAQS SSRSLNASQG RTFSTLARRL PATQKVFGQQ
RRGYATNTNP NPPLGKKNAS NDVPARVGLI GARGYTGQAL IDLLNSHPLM DLKHVSSREL
AGTELKGYTK RKIIYENLSP DDVGALEKDG AIDCWVMALP NGVCAPYVTA IDAAQNGQSV
IVDLSADYRF DDSSSFVYGL PELVKRSKIT QARRIANPGC FATGAQLGIA PILEHVGGLI
SVMGISGYSG AGTKPSQKND TSFLRDNLLP YSLTDHIHER EISTQLGTEV AFIPHVASWF
RGIHHTINIP LNKTMTSRDI RQLYQDRYAG EKLVKVVGEP PLVRNIMDKH GVEIGGFAVH
SSGKRVVVCA TIDNLNKGAA TQCLQNMNLA LGYAEYEGIP TM
//
