ARLY_ECODH
ID ARLY_ECODH Reviewed; 457 AA.
AC B1XBC5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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};
GN OrderedLocusNames=ECDH10B_4148;
OS Escherichia coli (strain K12 / DH10B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / DH10B;
RX PubMed=18245285; DOI=10.1128/jb.01695-07;
RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA Posfai G., Weinstock G.M., Blattner F.R.;
RT "The complete genome sequence of Escherichia coli DH10B: insights into the
RT biology of a laboratory workhorse.";
RL J. Bacteriol. 190:2597-2606(2008).
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; CP000948; ACB04971.1; -; Genomic_DNA.
DR RefSeq; WP_001230087.1; NC_010473.1.
DR AlphaFoldDB; B1XBC5; -.
DR SMR; B1XBC5; -.
DR KEGG; ecd:ECDH10B_4148; -.
DR HOGENOM; CLU_027272_2_3_6; -.
DR OMA; KKNPDVF; -.
DR BioCyc; ECOL316385:ECDH10B_RS21135-MON; -.
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..457
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000089080"
SQ SEQUENCE 457 AA; 50318 MW; 0109EF31675B9717 CRC64;
MALWGGRFTQ AADQRFKQFN DSLRFDYRLA EQDIVGSVAW SKALVTVGVL TAEEQAQLEE
ALNVLLEDVR ARPQQILESD AEDIHSWVEG KLIDKVGQLG KKLHTGRSRN DQVATDLKLW
CKDTVSELLT ANRQLQSALV ETAQNNQDAV MPGYTHLQRA QPVTFAHWCL AYVEMLARDE
SRLQDALKRL DVSPLGCGAL AGTAYEIDRE QLAGWLGFAS ATRNSLDSVS DRDHVLELLS
AAAIGMVHLS RFAEDLIFFN TGEAGFVELS DRVTSGSSLM PQKKNPDALE LIRGKCGRVQ
GALTGMMMTL KGLPLAYNKD MQEDKEGLFD ALDTWLDCLH MAALVLDGIQ VKRPRCQEAA
QQGYANATEL ADYLVAKGVP FREAHHIVGE AVVEAIRQGK PLEDLPLSEL QKFSQVIDED
VYPILSLQSC LDKRAAKGGV SPQQVAQAIA FAQARLG
