ARGE_DICDI
ID ARGE_DICDI Reviewed; 447 AA.
AC P54638; Q55GM1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Acetylornithine deacetylase;
DE EC=3.5.1.16;
DE AltName: Full=N-acetylornithinase;
DE Short=AO;
DE Short=Acetylornithinase;
DE Short=NAO;
GN Name=argE; Synonyms=aodD; ORFNames=DDB_G0267380;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AX3;
RA Lu C., Mann K., Marriott G.;
RT "Molecular cloning and sequence analysis of a member of the
RT argE/dapE/Acy1/CPG2/yscS protein family in Dictyostelium discoideum.";
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP DEVELOPMENTAL STAGE.
RX PubMed=11923193; DOI=10.1242/dev.129.7.1543;
RA Van Driessche N., Shaw C., Katoh M., Morio T., Sucgang R., Ibarra M.,
RA Kuwayama H., Saito T., Urushihara H., Maeda M., Takeuchi I., Ochiai H.,
RA Eaton W., Tollett J., Halter J., Kuspa A., Tanaka Y., Shaulsky G.;
RT "A transcriptional profile of multicellular development in Dictyostelium
RT discoideum.";
RL Development 129:1543-1552(2002).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=12912885; DOI=10.1128/ec.2.4.664-670.2003;
RA Iranfar N., Fuller D., Loomis W.F.;
RT "Genome-wide expression analyses of gene regulation during early
RT development of Dictyostelium discoideum.";
RL Eukaryot. Cell 2:664-670(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-acetyl-L-ornithine = acetate + L-ornithine;
CC Xref=Rhea:RHEA:15941, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:57805; EC=3.5.1.16;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) or Co(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine
CC from N(2)-acetyl-L-ornithine (linear): step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed during development. Expression levels
CC decrease steadily from the initiation of development until culmination.
CC Levels increase after 18 hours of development and peak at 22 hours,
CC after which they decrease again. {ECO:0000269|PubMed:11923193,
CC ECO:0000269|PubMed:12912885}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. ArgE subfamily.
CC {ECO:0000305}.
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DR EMBL; U23957; AAB04942.1; -; mRNA.
DR EMBL; AAFI02000003; EAL73142.1; -; Genomic_DNA.
DR RefSeq; XP_647163.1; XM_642071.1.
DR AlphaFoldDB; P54638; -.
DR SMR; P54638; -.
DR STRING; 44689.DDB0191165; -.
DR SWISS-2DPAGE; P54638; -.
DR PaxDb; P54638; -.
DR EnsemblProtists; EAL73142; EAL73142; DDB_G0267380.
DR GeneID; 8615966; -.
DR KEGG; ddi:DDB_G0267380; -.
DR dictyBase; DDB_G0267380; argE.
DR eggNOG; KOG2276; Eukaryota.
DR HOGENOM; CLU_051591_0_0_1; -.
DR InParanoid; P54638; -.
DR OMA; HAQNEYC; -.
DR PhylomeDB; P54638; -.
DR UniPathway; UPA00068; UER00110.
DR PRO; PR:P54638; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cobalt; Hydrolase;
KW Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..447
FT /note="Acetylornithine deacetylase"
FT /id="PRO_0000185256"
FT ACT_SITE 105
FT /evidence="ECO:0000250"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 53
FT /note="P -> S (in Ref. 1; AAB04942)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="E -> A (in Ref. 1; AAB04942)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="G -> GG (in Ref. 1; AAB04942)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="D -> N (in Ref. 1; AAB04942)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="R -> L (in Ref. 1; AAB04942)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 49070 MW; 115B0A123C1A3A7B CRC64;
MTKPVASYEL DEKRFLTLLG KLIGETENLQ NRPPALIPIE DNAGRHVIEA LTPYLKANGG
VLELEQVHCD PVNYPKRGNI IIEYPGTSKG TSSPKTISFV GSHLDVVPAD KTAWDRNPFQ
LIIEGDKLYG RGTTDCLGHV ALLTDLFIQL ATEKPALKHS IFAVFIVSEE NDEIPGIGVD
ALDHSGKMNP CKNGPVYWVD SADSQPTIGT GGAQTWNLTA HGKNMHSAMP YRTVNSVELV
NEALAEIQRR FYIDFKPHPK EAEYKFDCSS TMKPTLWKPI AGSYNTIPGE STICGDIRLT
PFYDMKEMRA KVEGYIKDIN ANITELRNRG PYSKYDVPAS EGVEPVKGSV SIEWLGEASA
GVACKLDSDG YKALGKATSE ILGSLTPVAT CGTLPLVRDL QDSGFDIQIT GFGKEETYHA
DNEYALLSDF KNAIKILSRT IDLLEKN
