ARLY_POLNS
ID ARLY_POLNS Reviewed; 472 AA.
AC B1XVG9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
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=Pnec_1201;
OS Polynucleobacter necessarius subsp. necessarius (strain STIR1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=452638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STIR1;
RX PubMed=24167248; DOI=10.1073/pnas.1316687110;
RA Boscaro V., Felletti M., Vannini C., Ackerman M.S., Chain P.S.,
RA Malfatti S., Vergez L.M., Shin M., Doak T.G., Lynch M., Petroni G.;
RT "Polynucleobacter necessarius, a model for genome reduction in both free-
RT living and symbiotic bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:18590-18595(2013).
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; CP001010; ACB44346.1; -; Genomic_DNA.
DR RefSeq; WP_012358109.1; NC_010531.1.
DR AlphaFoldDB; B1XVG9; -.
DR SMR; B1XVG9; -.
DR STRING; 452638.Pnec_1201; -.
DR EnsemblBacteria; ACB44346; ACB44346; Pnec_1201.
DR KEGG; pne:Pnec_1201; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_4; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 751464at2; -.
DR UniPathway; UPA00068; UER00114.
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.
FT CHAIN 1..472
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000116338"
SQ SEQUENCE 472 AA; 51851 MW; 90EE717498FCA7F8 CRC64;
MSSSNNSLNN KAQAWSARFA EPVDELVQRY TASIGFDQRF AMVDIAGSLA HAEMLATQKI
ISAQDLADIQ KGMAQIQSEI EAGQFEWQLA LEDVHLNIEA RLTQLVGDAG KRLHTGRSRN
DQVATDLRLW LRGSVDEIAL TLKSLRVALL DLAEKHASTI MPGHTHLQVA QPITFGHHLM
AYFEMFSRDA SRLADLRARF NRLPLGAAAL AGTTYPINRE QVAKALGFDG TCNNSLDAVS
DRDFAIEFCA FASILMMHVS RLSEELILWL SPRFGFIDLP DRFCTGSSIM PQKKNPDVPE
LARGKTGRVY GDLISLLTLM KGQPLAYNKD DQEDKEPLFD AVDTVQDTLR IFADMVPHIE
VKSEAMKKAA EEGFATATDL ADYLVKKGLA FRDAHEAVAH AVKACVGRNC MLTDLSLSEL
RFACGLDNRP ELIGDDVFVL LTVDGSVQSR QHAGGTAPAQ VLAAIKRGRA DL
