ARLY_MYCTO
ID ARLY_MYCTO Reviewed; 470 AA.
AC P9WPY6; L0TA28; P0A4Z0; P94994;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 33.
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=MT1697;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(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: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; AE000516; AAK45966.1; -; Genomic_DNA.
DR PIR; F70621; F70621.
DR RefSeq; WP_003917507.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WPY6; -.
DR SMR; P9WPY6; -.
DR EnsemblBacteria; AAK45966; AAK45966; MT1697.
DR KEGG; mtc:MT1697; -.
DR PATRIC; fig|83331.31.peg.1824; -.
DR HOGENOM; CLU_027272_2_2_11; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001020; 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.
FT CHAIN 1..470
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000426870"
SQ SEQUENCE 470 AA; 49790 MW; 1E250549DFC294AE CRC64;
MSTNEGSLWG GRFAGGPSDA LAALSKSTHF DWVLAPYDLT ASRAHTMVLF RAGLLTEEQR
DGLLAGLDSL AQDVADGSFG PLVTDEDVHS ALERGLIDRV GPDLGGRLRA GRSRNDQVAA
LFRMWLRDAV RRVATGVLDV VGALAEQAAA HPSAIMPGKT HLQSAQPILL AHHLLAHAHP
LLRDLDRIVD FDKRAAVSPY GSGALAGSSL GLDPDAIAAD LGFSAAADNS VDATAARDFA
AEAAFVFAMI AVDLSRLAED IIVWSSTEFG YVTLHDSWST GSSIMPQKKN PDIAELARGK
SGRLIGNLAG LLATLKAQPL AYNRDLQEDK EPVFDSVAQL ELLLPAMAGL VASLTFNVQR
MAELAPAGYT LATDLAEWLV RQGVPFRSAH EAAGAAVRAA EQRGVGLQEL TDDELAAISP
ELTPQVREVL TIEGSVSARD CRGGTAPGRV AEQLNAIGEA AERLRRQLVR