ARLY_PROMT
ID ARLY_PROMT Reviewed; 463 AA.
AC Q46I50;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-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=PMN2A_1339;
OS Prochlorococcus marinus (strain NATL2A).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59920;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL2A;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(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; CP000095; AAZ58828.1; -; Genomic_DNA.
DR RefSeq; WP_011293972.1; NC_007335.2.
DR AlphaFoldDB; Q46I50; -.
DR SMR; Q46I50; -.
DR STRING; 59920.PMN2A_1339; -.
DR EnsemblBacteria; AAZ58828; AAZ58828; PMN2A_1339.
DR KEGG; pmn:PMN2A_1339; -.
DR HOGENOM; CLU_027272_2_3_3; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 751464at2; -.
DR PhylomeDB; Q46I50; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000002535; 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..463
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000240750"
SQ SEQUENCE 463 AA; 52533 MW; 932135C807636B13 CRC64;
MEKALSKTWS ERFDKGLNPF IEKFNASIEF DICLLEEDLD GSIAHARMLG IQGIITKEEA
LRLENGLQQI RKEASDGLFH PVISDEDVHF AVEKKLIDLI GPVGKKLHTG RSRNDQVGTD
LRLWLRKRID EIDMDLVRLQ KSLFLLAEEN LYTLIPGYTH LQRAQPLSLA HHLLAYIEMA
QRDRNRLKDV RKRVNISPLG AAALAGTSIS ISRKITSSEL HFQGIYSNSL DAVSDRDFVV
EFLGASSLIM AHLSRLSEEV ILWASEEFAF IQLTDRCATG SSLMPQKKNP DVPELVRGKS
GRVFGHLQAM LTMIKGLPLA YNKDFQEDKE AIFDSVKTVK NSLIAISILF EEGLIFRKER
LNQAVSSDFS NATDVADYLV AKDIPFREAY QLVGRIVKTS LEEGILLKDI PLERWKTFHK
FFEKDIYEKL LPSSVVESRL SAGGTGFERV QEQLLSWREK LFN
