ID D5G7N7_TUBMM Unreviewed; 655 AA.
AC D5G7N7;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=(Perigord truffle) hypothetical protein {ECO:0000313|EMBL:CAZ80530.1};
GN ORFNames=GSTUM_00004655001 {ECO:0000313|EMBL:CAZ80530.1};
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061 {ECO:0000313|EMBL:CAZ80530.1, ECO:0000313|Proteomes:UP000006911};
RN [1] {ECO:0000313|EMBL:CAZ80530.1, ECO:0000313|Proteomes:UP000006911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28 {ECO:0000313|EMBL:CAZ80530.1,
RC ECO:0000313|Proteomes:UP000006911};
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004828}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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DR EMBL; FN430031; CAZ80530.1; -; Genomic_DNA.
DR RefSeq; XP_002836339.1; XM_002836293.1.
DR AlphaFoldDB; D5G7N7; -.
DR STRING; 656061.D5G7N7; -.
DR EnsemblFungi; CAZ80530; CAZ80530; GSTUM_00004655001.
DR GeneID; 9187009; -.
DR KEGG; tml:GSTUM_00004655001; -.
DR eggNOG; KOG2436; Eukaryota.
DR eggNOG; KOG4354; Eukaryota.
DR HOGENOM; CLU_006384_4_0_1; -.
DR InParanoid; D5G7N7; -.
DR OMA; GSKATIC; -.
DR OrthoDB; 987250at2759; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000006911; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:EnsemblFungi.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:EnsemblFungi.
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; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR041734; NAGK-fArgBP.
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 SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51731; GNAT_NAGS; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Reference proteome {ECO:0000313|Proteomes:UP000006911};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 340..493
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51731"
SQ SEQUENCE 655 AA; 71678 MW; A99B4639E89511BA CRC64;
MLSGLRNSSR RSVRLPTFRN LRVIRPAAPI PSSSSTCPLR ITASSYATTS LSPSPLSTRS
TVIQLLNNIG SKREVEQYLS HFTSVQSQQF AVIKVGGAII TEHLDSLSNS LSFLNHVGLF
PVVVHGAGPQ LNKMLEAAGV EPQFEDGIRV TDGKTLALAR QLFLDENLKL VEALEKLGVR
ARPITGGVFQ ADYLDRKKYD LVGKITSVDK RPIEAAIKAG CLPILTSTAE TAEGQLLNVN
ADIAAGELAR ALQPLKIVYL SEKGGLFNGE TNEKISTINL DEEYAGLMEQ WWCRFGTRLK
IKEIKELLDG LPRTSSVAII ATEDLQKELF TDTGAGTLIR RGNKLTAMSS IEGFEDRTRL
EEVLGREKND VSEYLSFLQT TKFKAYADEP LEVLAIVLPS ESTNEPARLD FFSSTKAGWL
GNVADNVFNL IKKEYPRLVW SVRQGDGQLG WHFDKSQGSF NHGGQVHFWY GYEGPEEVKS
LIGGFLADAG SRESGKSEGA VTGVKQQVRG FASTNPNPPL GSSNATNNKP SKVALIGARG
YTGQALITLI NSHPHFDLTH VSSRELAGKK LEGYTKDGKE IVYQNLGVED IRRMEENGEV
DCWVMALPNG VCKPFVDAVE DVGKGKSVIV DLSADFRFDS KWTYGLPGIL CPERP
//
