ARLY_EHRCJ
ID ARLY_EHRCJ Reviewed; 471 AA.
AC Q3YSS4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
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=Ecaj_0180;
OS Ehrlichia canis (strain Jake).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=269484;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jake;
RX PubMed=16707693; DOI=10.1128/jb.01837-05;
RA Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT "The genome of the obligately intracellular bacterium Ehrlichia canis
RT reveals themes of complex membrane structure and immune evasion
RT strategies.";
RL J. Bacteriol. 188:4015-4023(2006).
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; CP000107; AAZ68231.1; -; Genomic_DNA.
DR RefSeq; WP_011304309.1; NC_007354.1.
DR AlphaFoldDB; Q3YSS4; -.
DR SMR; Q3YSS4; -.
DR STRING; 269484.Ecaj_0180; -.
DR PRIDE; Q3YSS4; -.
DR EnsemblBacteria; AAZ68231; AAZ68231; Ecaj_0180.
DR KEGG; ecn:Ecaj_0180; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_5; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 751464at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000000435; 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..471
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000240727"
SQ SEQUENCE 471 AA; 53254 MW; 86243E51CA7453C4 CRC64;
MKNPLWGGRF TTSSSDIMKK INESISFDKT LYEEDIAGSI AHCKMLVNQR IISKYEGQLI
IHGLEVIQNQ ISSGTFEFST DLEDIHMNIE HNLKKMVGNI AGKLHTARSR NDQVATDFKL
WIRKSIVKIE HYLHELQDTI INLAESHYNT IMPGFTHLQI AQPVTLGHHL MAYFEMFKRD
FSRWQDLYKR MNQCPLGSAA LAGTSFPIDR HFVAQELGFY SPTENSIDAV SDRDYAIEFL
SNASICIMHL SRLAEEIILW CSYNFKFITL SDNITTGSSI MPQKKNPDAA ELIRGKTGRI
FASLNQILVV MKGLPLAYSK DMQEDKEALF DATNNLMLCI EAMNNMLSNI IINKNNMLKA
AEHDYSTATD LADWLVKNLN LSFREAHETT GQIVKLAEHN QCKLHELTLE QIKTIIPSIN
DTVFSVLSVE NSVASRTSYG GTAPTNVIEA IKKGKAYLSN IKFSQTDKNN I