ID R7S5M3_PUNST Unreviewed; 896 AA.
AC R7S5M3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Acetylglutamate kinase ARG6 {ECO:0000313|EMBL:EIN04731.1};
GN ORFNames=PUNSTDRAFT_138376 {ECO:0000313|EMBL:EIN04731.1};
OS Punctularia strigosozonata (strain HHB-11173) (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Corticiales; Punctulariaceae; Punctularia.
OX NCBI_TaxID=741275 {ECO:0000313|EMBL:EIN04731.1, ECO:0000313|Proteomes:UP000054196};
RN [1] {ECO:0000313|Proteomes:UP000054196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-11173 SS5 {ECO:0000313|Proteomes:UP000054196};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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}.
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DR EMBL; JH687553; EIN04731.1; -; Genomic_DNA.
DR RefSeq; XP_007388124.1; XM_007388062.1.
DR AlphaFoldDB; R7S5M3; -.
DR GeneID; 18880059; -.
DR KEGG; psq:PUNSTDRAFT_138376; -.
DR eggNOG; KOG2436; Eukaryota.
DR eggNOG; KOG4354; Eukaryota.
DR HOGENOM; CLU_006384_4_0_1; -.
DR OMA; IAFIPHV; -.
DR OrthoDB; 987250at2759; -.
DR UniPathway; UPA00068; UER00107.
DR Proteomes; UP000054196; 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:UP000054196};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036440};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 338..495
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51731"
FT ACT_SITE 688
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 896 AA; 96694 MW; F63343472578BD66 CRC64;
MLSATSRAVR ATASRAAVPK PAAVAKACNA VVVKRTIRGI HSASSSIQTD RDTITRLLYS
IGTKKEVERY LRIFSSSSHP SNPAKFAVIK IGGAVLDELD ELAHALSFLY RVGLYPVVLH
GAGPQLNEIL EREGVVPDYI DGIRVTDPKT LGIARRVFLE ENLKLVAALE SLGTRARPIT
SGVFQADYLD RAKYNLVGKI TKIDRRPIEA SIRAGALPIL TSLAETTEGQ ILNVNADVAA
GELAKEFEPL KIVFLNEKGG LFHGVTGEKL DVINLDEEYD ELMRQPWVKY GTKLKLREFK
ELLDVLPRSS SVAVISASSL QKELFTDSGA GTLIRRGYKL FKHGAVDQVG RDRLREVIKE
RDIDVLAGLT SPGKVLEGIE KLGAGNYTIY GDEPLDALAV VSHPPGKVPI LTRLFASRSG
VLNNVLDNVF DAIRKDHRRL FWTAPSDDEN RAWHFERAEG SFIRGGRGLF WYGVGDVGEV
EKIVRGFEEE GRIERAYLPV GPAKAHRAAA SGIGGAKAFS TLARQVPGSS RGYATAASVP
PNFETKTRNV ALVGARGFTG QALTSLFDKH PYINLTHVSS RQLKGFSLEG YNKSKVTYSD
LSVKDVEKME KDGEVDAWVM ALPNGVCKPF VDAVDAGAAA KSKDGKEGGV IVDLSADHRF
EDGWTYGLPE LYSREQVKTA KRVSNPGCYA TAVQMLLAPL LPLLPSHPAV LPTVFGISGY
SGAGTVSGPT DEQGRPTTLP KVSPQSLKGG IRPYSLTGHI HEREAGRHLA SLLPADHAGE
FKVAFTPAVA PWFSGILATA SVPLAKSVSA KEVWALYEER YAGEKLVRMK KEGVVELADV
ENKHGFVLGG VQVAAGGERA VVVGGLDNLL KGAATQCLQN LNLALGYDEY AGIPLD
//
