ARLY_DEHM1
ID ARLY_DEHM1 Reviewed; 461 AA.
AC Q3Z726;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 102.
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=DET1261;
OS Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS (Dehalococcoides ethenogenes (strain 195)).
OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=243164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX PubMed=15637277; DOI=10.1126/science.1102226;
RA Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA Zinder S.H., Heidelberg J.F.;
RT "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT ethenogenes.";
RL Science 307:105-108(2005).
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; CP000027; AAW39469.1; -; Genomic_DNA.
DR RefSeq; WP_010936950.1; NC_002936.3.
DR AlphaFoldDB; Q3Z726; -.
DR SMR; Q3Z726; -.
DR STRING; 243164.DET1261; -.
DR PRIDE; Q3Z726; -.
DR EnsemblBacteria; AAW39469; AAW39469; DET1261.
DR KEGG; det:DET1261; -.
DR PATRIC; fig|243164.10.peg.1190; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_0; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 751464at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000008289; 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_0000240724"
SQ SEQUENCE 461 AA; 51044 MW; 0F670C102EB1FA36 CRC64;
MSHIRSRFSK PADELVVRYT TSLPFDWRLY QEDIKCSTAH ARMLGKQSII SAGDSQSIIN
GLSDILTEIE TGSFVFKPEM EDIHMAIEGR LFELIGEAAG RLHTARSRND QVATDVHLFV
KNTCTSTINK IRTLQGALLK QAEAHQQTAL PGYTHLQVAQ PVLLSHHLLA YFEMLERDCG
RFTDAKKRSD VMPLGSGALA GVPYPLDRKM VAEELGFTAI SQNSLDAVSE RDFVLEYLSD
AAICQMHLSR LSEEMVIWSS AEYAFVELDD AYTTGSSIMP QKKNPDVAEL CRGKTGRVYG
SLNTMLTVMK GLPLSYNRDL QEDKEPLFEC ADTLGDSLEV FAGMIKTATF KPERMLRALE
KGYVLATDIA DYLVGKGESF RSSHGIVARL VSYAISQNKT FGELSLEEYR QFSNLFGNDI
YAVDIKSALN ARNLTGGTAP KQIAQAIARA KKILAEAGVK N