ID U1GUZ8_ENDPU Unreviewed; 1020 AA.
AC U1GUZ8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Arginine-requiring protein 2 {ECO:0000256|ARBA:ARBA00030322};
GN ORFNames=EPUS_04150 {ECO:0000313|EMBL:ERF76293.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF76293.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 3/4.
CC {ECO:0000256|ARBA:ARBA00004862}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAGSA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007239}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the acetylglutamate
CC kinase family. {ECO:0000256|ARBA:ARBA00006830}.
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DR EMBL; KE720769; ERF76293.1; -; Genomic_DNA.
DR RefSeq; XP_007786334.1; XM_007788144.1.
DR AlphaFoldDB; U1GUZ8; -.
DR GeneID; 19239183; -.
DR eggNOG; KOG0860; Eukaryota.
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; UP000019373; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003991; F:acetylglutamate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0070401; F:NADP+ binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd04252; AAK_NAGK-fArgBP; 1.
DR CDD; cd04263; DUF619-NAGK-FABP; 1.
DR Gene3D; 1.20.5.110; -; 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; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR001388; Synaptobrevin-like.
DR InterPro; IPR042855; V_SNARE_CC.
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; PF00957; Synaptobrevin; 1.
DR PRINTS; PR00219; SYNAPTOBREVN.
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 SUPFAM; SSF58038; SNARE fusion complex; 1.
DR PROSITE; PS01224; ARGC; 1.
DR PROSITE; PS51731; GNAT_NAGS; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU00290};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000019373};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 88..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..84
FT /note="V-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50892"
FT DOMAIN 473..626
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51731"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 837
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10010"
SQ SEQUENCE 1020 AA; 113364 MW; 0DC73E6DFC2203D7 CRC64;
MADREPAYDP WPAGGSAEDR HQAKMDRINK DMDAAKAAMN DNIRLANTRG ENLDTLRDKT
DHLQNQSQSF RKGANRVRKQ MWWKDMKMRI CIIVGIIILL IVIIVPSERD QIGQAYRYNC
SCRMSVSSMI AVRPASQAAS QAVRCLVRSC ASPALRQTCK LSQRSSLLYL AHRDYSSPSE
HHLSTRSTVV QLLSNIGSKR EVQQYLSHFS SVSSQQFAVI KVGGAIITEH LQTLSSALAF
LNHVGLYPVV VHGAGPQLNK LLEDSGVKPQ FEDGIRITDP KTLGVARALF LEENLKLVEE
LERLGVRARP ITSGVFSADY LDKEKYNLVG KINKVDNRPI EAAIQAGCLP ILTSMAETSA
GQVLNVNADV AAGELARSIQ PLKIVYLSEK GGLFNGDTKE KISAINLDEE YDHLMTQWWV
RHGTRLKIKE MKELLTDLPR SSSVAIIHPA DLQKELFTDT GAGTLIRRGN KVHVNTSLSE
FEDLEKLKEV LVRDREGLDS KAVVDRYLKS LEDRDFRAYF DEPMEALAIV LPPQQNASIA
HLATFTITKA GWLTNVADNV FASIKKDYPM LMWTVKEDDE NLTWFFDKAD GSLSKSGEVL
FWYGIEKSDD VKELMLEFTK HGRKMFGDIN LESRLHRAFR TVSNVMASAT NVQQARAYSS
AASPLHSYRL IRRQLAQTSP GRSYATTTNP NPPLGDKNNS NSRPAKVALI GARGYTGQAL
IDLLNHHPNM DLQHVSSREL AGQKLKGYEK KEITYENLSA EDVRRMAEDG QIDCWVMALP
NGVCKPFVDA INSGSKNSLV IDLSADYRFD SEWTYGLPEL IDRSRIAKAT RISNPGCYAT
AAQLGIAPLI PYLGGQPTVF GVSGYSGAGT RPSPKNDVQN LTNNIIPYSL TDHIHEKEIS
AQLQEDIAFV PHVAVWFQGI HHTISIPLKD EMSSRDIRTL YQDRYAGEKL VRIIGEPPLV
KNIAGRHGIE IGGFAVHSSG KRVVICATID NLLKGAATQC LQNMNLALGY SEYEGIPLER
//
