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ARLY_METPP
ID   ARLY_METPP              Reviewed;         467 AA.
AC   A2SET3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=Mpe_A1111;
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX   NCBI_TaxID=420662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX   PubMed=17158667; DOI=10.1128/jb.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
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; CP000555; ABM94072.1; -; Genomic_DNA.
DR   RefSeq; WP_011828709.1; NC_008825.1.
DR   AlphaFoldDB; A2SET3; -.
DR   SMR; A2SET3; -.
DR   STRING; 420662.Mpe_A1111; -.
DR   EnsemblBacteria; ABM94072; ABM94072; Mpe_A1111.
DR   KEGG; mpt:Mpe_A1111; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_4; -.
DR   OMA; KKNPDVF; -.
DR   OrthoDB; 751464at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000000366; 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..467
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_0000321442"
SQ   SEQUENCE   467 AA;  51192 MW;  344DBDA4400A6ED4 CRC64;
     MSNDNQLDKK SQAWSALFSE PMSELVKRYT ASVDFDQRLW RADIDGSLAH AEMLAAQGIL
     TAEDHAAIVR GMAQVVAEIE SGAFEWKLDL EDVHLNIEAR LTQLVGDAGK RLHTGRSRND
     QVATDVRLWL RGEIDAIGAL LSALQRALVD VAEPNAEVIL PGFTHLQVAQ PVSFGHHLLA
     YVEMFARDAE RLLDVRRRVN RLPLGAAALA GTSYPLDRER VARTLGFDGV CQNSLDAVSD
     RDFAIEFTAA ASLCMVHVSR LSEELILWMS QSFGFIDLAD RFCTGSSIMP QKKNPDVPEL
     ARGKTGRVVG HLMALITLMK GQPLAYNKDN QEDKEPLFDT VDTLKDTLRI FAELVGGISV
     KPEAMERAAL KGYATATDLA DYLVKKGLPF RDAHEVVAHA VKTAIAQGRD LSELPLPALQ
     AFHPAITDDV HAALTLRGSL DARQVLGGTA PAQVRFQIAR HRTRLGS
 
 
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