ARLY_SCHPO
ID ARLY_SCHPO Reviewed; 461 AA.
AC P40369; O94571;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Argininosuccinate lyase;
DE Short=ASAL;
DE EC=4.3.2.1 {ECO:0000305|PubMed:1868575};
DE AltName: Full=Arginosuccinase;
GN Name=arg7; ORFNames=SPBC1773.14;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=1868575; DOI=10.1007/bf00355051;
RA Loppes R., Michels R., Decroupette I., Joris B.;
RT "Sequence analysis of the ARG7 gene of Schizosaccharomyces pombe coding for
RT argininosuccinate lyase. Expression of the gene in Saccharomyces
RT cerevisiae.";
RL Curr. Genet. 19:255-260(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(N(omega)-L-arginino)succinate = fumarate + L-arginine;
CC Xref=Rhea:RHEA:24020, ChEBI:CHEBI:29806, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:57472; EC=4.3.2.1; Evidence={ECO:0000305|PubMed:1868575};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 3/3.
CC {ECO:0000305|PubMed:1868575}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000305}.
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DR EMBL; X63262; CAA44915.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA21919.1; -; Genomic_DNA.
DR PIR; S32580; S32580.
DR PIR; T39679; T39679.
DR RefSeq; NP_595129.1; NM_001021036.2.
DR AlphaFoldDB; P40369; -.
DR SMR; P40369; -.
DR BioGRID; 276524; 10.
DR STRING; 4896.SPBC1773.14.1; -.
DR iPTMnet; P40369; -.
DR SwissPalm; P40369; -.
DR MaxQB; P40369; -.
DR PaxDb; P40369; -.
DR PRIDE; P40369; -.
DR EnsemblFungi; SPBC1773.14.1; SPBC1773.14.1:pep; SPBC1773.14.
DR GeneID; 2539980; -.
DR KEGG; spo:SPBC1773.14; -.
DR PomBase; SPBC1773.14; arg7.
DR VEuPathDB; FungiDB:SPBC1773.14; -.
DR eggNOG; KOG1316; Eukaryota.
DR HOGENOM; CLU_027272_2_1_1; -.
DR InParanoid; P40369; -.
DR OMA; DFIYCCS; -.
DR PhylomeDB; P40369; -.
DR UniPathway; UPA00068; UER00114.
DR PRO; PR:P40369; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IMP:PomBase.
DR GO; GO:0006526; P:arginine biosynthetic process; IMP:PomBase.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR GO; GO:0000050; P:urea cycle; IC:PomBase.
DR CDD; cd01359; Argininosuccinate_lyase; 1.
DR Gene3D; 1.10.275.10; -; 1.
DR HAMAP; MF_00006; Arg_succ_lyase; 1.
DR InterPro; IPR029419; Arg_succ_lyase_C.
DR InterPro; IPR009049; Argininosuccinate_lyase.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR PANTHER; PTHR43814; PTHR43814; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR00838; argH; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Arginine biosynthesis; Lyase; Reference proteome.
FT CHAIN 1..461
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137725"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT ACT_SITE 282
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT BINDING 28
FT /ligand="2-(N(omega)-L-arginino)succinate"
FT /ligand_id="ChEBI:CHEBI:57472"
FT /ligand_note="ligand shared between tetrameric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT BINDING 115
FT /ligand="2-(N(omega)-L-arginino)succinate"
FT /ligand_id="ChEBI:CHEBI:57472"
FT /ligand_note="ligand shared between tetrameric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT BINDING 160
FT /ligand="2-(N(omega)-L-arginino)succinate"
FT /ligand_id="ChEBI:CHEBI:57472"
FT /ligand_note="ligand shared between tetrameric partners"
FT /note="in chain C"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT BINDING 290
FT /ligand="2-(N(omega)-L-arginino)succinate"
FT /ligand_id="ChEBI:CHEBI:57472"
FT /ligand_note="ligand shared between tetrameric partners"
FT /note="in chain B"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT BINDING 322
FT /ligand="2-(N(omega)-L-arginino)succinate"
FT /ligand_id="ChEBI:CHEBI:57472"
FT /ligand_note="ligand shared between tetrameric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT BINDING 327
FT /ligand="2-(N(omega)-L-arginino)succinate"
FT /ligand_id="ChEBI:CHEBI:57472"
FT /ligand_note="ligand shared between tetrameric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT BINDING 330
FT /ligand="2-(N(omega)-L-arginino)succinate"
FT /ligand_id="ChEBI:CHEBI:57472"
FT /ligand_note="ligand shared between tetrameric partners"
FT /note="in chain A"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT SITE 295
FT /note="Increases basicity of active site His"
FT /evidence="ECO:0000250|UniProtKB:P24058"
FT CONFLICT 199..200
FT /note="PL -> TA (in Ref. 1; CAA44915)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="R -> P (in Ref. 1; CAA44915)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="F -> S (in Ref. 1; CAA44915)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="A -> AS (in Ref. 1; CAA44915)"
FT /evidence="ECO:0000305"
FT CONFLICT 451..461
FT /note="EQIEHIRSAIL -> DNRAYTISNS (in Ref. 1; CAA44915)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 51738 MW; 60AA6D072C58FB86 CRC64;
MAEKSSKKLW GGRFSGATDP LMAEFNKSIY SGKEMCEEDV IGSMAYAKAL CQKNVISEEE
LNSILKGLEQ IQREWNSGQF VLEPSDEDVH TANERRLTEI IGDVAGKLHT GRSRNDQVTT
DLRLWLCRKI KEVEVYVINL LKVFTNRAEM EIDVIMSGYT HLQRAQPVRW SHFLMSHALP
LLGDLGRLRQ LYTRVSQLPL GAGALAGNPF NVDREFLRKE LGFEGIIMNS MNAVGDRDFV
IEFMFWAGMV MLHISRFAED LIIYSSSEFG FVTLSDAYST GSSIMPQKKN PDSLELLRGK
SGRVLGDMIG LMITVKGTPT TYNKDLQEDK EPLFDAFKTV SDSLQILTGV VSTLTINPTK
IAESLTPDLL ATDLAEYLVR KGLPFRQTHH ISGSAVRMAE ERNTTLDKLS VSDLQSLHPL
FDEDVSKVFN YEESVEKRCS IGGTAKHCVQ EQIEHIRSAI L
