ID A0A1E5RUT2_HANUV Unreviewed; 1196 AA.
AC A0A1E5RUT2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03124};
DE Includes:
DE RecName: Full=Glutamate N-acetyltransferase {ECO:0000256|HAMAP-Rule:MF_03124};
DE Short=GAT {ECO:0000256|HAMAP-Rule:MF_03124};
DE EC=2.3.1.35 {ECO:0000256|HAMAP-Rule:MF_03124};
DE AltName: Full=Ornithine acetyltransferase {ECO:0000256|HAMAP-Rule:MF_03124};
DE Short=OATase {ECO:0000256|HAMAP-Rule:MF_03124};
DE AltName: Full=Ornithine transacetylase {ECO:0000256|HAMAP-Rule:MF_03124};
DE Includes:
DE RecName: Full=Amino-acid acetyltransferase {ECO:0000256|HAMAP-Rule:MF_03124};
DE EC=2.3.1.1 {ECO:0000256|HAMAP-Rule:MF_03124};
DE AltName: Full=N-acetylglutamate synthase {ECO:0000256|HAMAP-Rule:MF_03124};
DE Short=AGS {ECO:0000256|HAMAP-Rule:MF_03124};
DE Contains:
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ alpha chain {ECO:0000256|HAMAP-Rule:MF_03124};
DE Contains:
DE RecName: Full=Arginine biosynthesis bifunctional protein ArgJ beta chain {ECO:0000256|HAMAP-Rule:MF_03124};
GN ORFNames=AWRI3580_g1539 {ECO:0000313|EMBL:OEJ90568.1};
OS Hanseniaspora uvarum (Yeast) (Kloeckera apiculata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycodaceae; Hanseniaspora.
OX NCBI_TaxID=29833 {ECO:0000313|EMBL:OEJ90568.1, ECO:0000313|Proteomes:UP000095358};
RN [1] {ECO:0000313|Proteomes:UP000095358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI3580 {ECO:0000313|Proteomes:UP000095358};
RX PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT "Genome sequences of three species of Hanseniaspora isolated from
RT spontaneous wine fermentations.";
RL Genome Announc. 4:E01287-E01287(2016).
CC -!- FUNCTION: Catalyzes two activities which are involved in the cyclic
CC version of arginine biosynthesis: the synthesis of acetylglutamate from
CC glutamate and acetyl-CoA, and of ornithine by transacetylation between
CC acetylornithine and glutamate. {ECO:0000256|HAMAP-Rule:MF_03124}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-
CC acetyl-L-glutamate; Xref=Rhea:RHEA:15349, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:44337, ChEBI:CHEBI:46911, ChEBI:CHEBI:57805; EC=2.3.1.35;
CC Evidence={ECO:0000256|ARBA:ARBA00000498, ECO:0000256|HAMAP-
CC Rule:MF_03124};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate;
CC Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03124};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine
CC and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine
CC (cyclic): step 1/1. {ECO:0000256|HAMAP-Rule:MF_03124}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC L-ornithine from L-glutamate: step 1/4. {ECO:0000256|HAMAP-
CC Rule:MF_03124}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000256|HAMAP-
CC Rule:MF_03124}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000256|HAMAP-
CC Rule:MF_03124}.
CC -!- PTM: The alpha and beta chains are autoproteolytically processed from a
CC single precursor protein within the mitochondrion. {ECO:0000256|HAMAP-
CC Rule:MF_03124}.
CC -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000256|ARBA:ARBA00006774,
CC ECO:0000256|HAMAP-Rule:MF_03124}.
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:OEJ90568.1}.
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DR EMBL; LPNN01000003; OEJ90568.1; -; Genomic_DNA.
DR STRING; 29833.A0A1E5RUT2; -.
DR VEuPathDB; FungiDB:AWRI3580_g1539; -.
DR OrthoDB; 3682876at2759; -.
DR UniPathway; UPA00068; UER00106.
DR Proteomes; UP000095358; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004358; F:glutamate N-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0022613; P:ribonucleoprotein complex biogenesis; IEA:UniProt.
DR CDD; cd17917; DEXHc_RHA-like; 1.
DR CDD; cd02152; OAT; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.30.2330.10; arginine biosynthesis bifunctional protein suprefamily; 1.
DR Gene3D; 3.10.20.340; ArgJ beta chain, C-terminal domain; 1.
DR Gene3D; 3.60.70.12; L-amino peptidase D-ALA esterase/amidase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_01106; ArgJ; 1.
DR InterPro; IPR002813; Arg_biosynth_ArgJ.
DR InterPro; IPR016117; ArgJ-like_dom_sf.
DR InterPro; IPR042195; ArgJ_beta_C.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00120; ArgJ; 1.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF118; ATP-DEPENDENT RNA HELICASE DHX33; 1.
DR Pfam; PF01960; ArgJ; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF56266; DmpA/ArgJ-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|HAMAP-
KW Rule:MF_03124}; Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03124};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_03124}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813, ECO:0000256|HAMAP-
KW Rule:MF_03124}; Helicase {ECO:0000313|EMBL:OEJ90568.1};
KW Hydrolase {ECO:0000313|EMBL:OEJ90568.1};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03124};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_03124}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000095358};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03124}.
FT CHAIN 1..969
FT /note="Arginine biosynthesis bifunctional protein ArgJ
FT alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT /id="PRO_5023342816"
FT CHAIN 970..1196
FT /note="Arginine biosynthesis bifunctional protein ArgJ beta
FT chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT /id="PRO_5023342815"
FT DOMAIN 98..263
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 288..474
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 970
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 932
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 959
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 970
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 1056
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 1191
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT BINDING 1196
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT SITE 895
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT SITE 896
FT /note="Involved in the stabilization of negative charge on
FT the oxyanion by the formation of the oxyanion hole"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
FT SITE 969..970
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03124"
SQ SEQUENCE 1196 AA; 133676 MW; A4B5EAED041B21A5 CRC64;
MATSVSHSSG KNQRKKNSVN PFRNKLKNKQ NDKKKPVIFK DFDDDDNEDE FLDNLIQAED
SKPKYQKLTK RDLKDRAXEI LEKQRKRLPV YQNKDEIMSY VKKNQVTVLI GETGSGKSTQ
IPQFLIDSVK SGKKIAVTQP RRVAAISLAG RVAAEYGCII GDEVGYSVRF DNRTNDKKTK
LKYLTDGMLL RELMMDKSLA QYEYLIIDEA HERTILTDLL LGFIKGLLNG PRKNDLKVIV
MSATLQADKF SKFFNDAPIL FVKGRTYPVE NFHLSHKDSE DQTDIVESMI RSVIQVNSSE
PFGGDILCFL PGQEEIDKAV AILQKISPIL KDSYIKQKLK IPEIVPLPLY AALTPAKQLL
VFNKLNXNKF QRKIILSTNI AETSVTIPGV KYVVDSGLRK VKIWRHELGL STLLTVPVSR
ASCQQRSGRA GRESEGKCFR LFKEHDFENL PVQSESEIIR CDISNPLLIL KKVGVKDILN
WSWLESPGKN AIVIGLEELY SLGALNDSGD LTEKGEKMAL LPLAPHLSNV LLEAMERXCI
SAVLDIVACL SVENLLLNPN PDIRDVVNEK RYQSATLGRR YGDLIMLKEF YDIFIGLDSV
PEQKQWCQEM SITYRGFQNV IKIRKQLKEY LKKIDANVEK NEKFNNKEKN SSVADESDDE
DFIETNDKKI DVESVLKCFL YGFVKNTAIG MPDRSYRTTT TGEPISIHPS SMMFSKKDNP
GIMYTEYVFT SKGFARNVSR IELXWLQEVA MGVRKFKPLN MKFTSTLLKT KAPIDKYSLY
VPKTGVFPKQ FEVGSLATGV KKNGNLDLGI IVNKNLSKKS TSSAVFTTNR FKAAPVLKSK
EVLESNNFEG INAIVVNSGC ANSMTGEVGM KDAEKMCELV NDKLNLKNQT LIMSTGVIGQ
KLQMDKIXKG INDIQFGSGF EDWLNMAKSI CTTDTFPKLI TSQFKLKNGK VYTLTGIAKG
AGMICPNMAT LLGYVVTDLP ISSRGIKKIL SFAGERSFNC ISVDGDMSTN DTICMIANGA
VETETIDIDS PDFEDVSKHV TSFAQQLAQL VVRDGEGATK FVTVKVTKSK TFEDAKIIAE
TISNSSLVKT ALYGEDANWG RILCAVGYSK TNSYDSLDEN KLNVKFVATD GSSPSELPLL
INGVPNLKVD EARASEILAL NDLEIVVELN TGDEECNFWT CDLTHEYVTI NGDYRS
//
