ARLY_TOLAT
ID ARLY_TOLAT Reviewed; 461 AA.
AC C4L7S8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Argininosuccinate lyase {ECO:0000255|HAMAP-Rule:MF_00006};
DE Short=ASAL {ECO:0000255|HAMAP-Rule:MF_00006};
DE EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006};
DE AltName: Full=Arginosuccinase {ECO:0000255|HAMAP-Rule:MF_00006};
GN Name=argH {ECO:0000255|HAMAP-Rule:MF_00006}; OrderedLocusNames=Tola_0097;
OS Tolumonas auensis (strain DSM 9187 / TA4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Tolumonas.
OX NCBI_TaxID=595494;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9187 / TA4;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S.,
RA Beller H.;
RT "Complete sequence of Tolumonas auensis DSM 9187.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-
CC Rule:MF_00006};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 3/3. {ECO:0000255|HAMAP-
CC Rule:MF_00006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00006}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00006}.
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DR EMBL; CP001616; ACQ91727.1; -; Genomic_DNA.
DR RefSeq; WP_012728327.1; NC_012691.1.
DR AlphaFoldDB; C4L7S8; -.
DR SMR; C4L7S8; -.
DR STRING; 595494.Tola_0097; -.
DR EnsemblBacteria; ACQ91727; ACQ91727; Tola_0097.
DR KEGG; tau:Tola_0097; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_6; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 751464at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000009073; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase;
KW Reference proteome.
FT CHAIN 1..461
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000201706"
SQ SEQUENCE 461 AA; 50800 MW; E450EB0DB7CD0A94 CRC64;
MALWGGRFSQ AADTRFKQFN DSLRFDYRLA EQDIVGSIGW SKALVSVGIL TAEEQAKLEV
ALLALKAEVE ADPEQILRSD AEDIHSWVEG KLIERVGDLG KKLHTGRSRN DQVATDLKLW
CKQQGNLLLD SIHGLQTKLV ATARQYQTTV LPGYTHLQRA QPVTFSHWAL AYVEMLDRDY
SRLQDALKRL NTSPLGSGAL AGTAYAIDRQ VLALDLGFDR ATRNSLDSVS DRDHVIELMS
SAALSMIHLS RFAEDLIFYA SGEAGFIELS DKVTSGSSLM PQKKNPDALE LIRGKTGRVA
GALNGMLMTL KALPLAYNKD MQEDKEGLFD ALDTWHDCLD MAQLVLEDLK VNEPVTKAAA
MGGYSNATEL ADYLVAKGIP FREAHHIVGE AVVYAITQQK PLEDLSVAEF KQFNAVIADD
VYPILSLEST LAKRQALGGV CAEQIAFALQ QAEQHLSTRH K