ARLY_PROM3
ID ARLY_PROM3 Reviewed; 470 AA.
AC A2C5K9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=P9303_00121;
OS Prochlorococcus marinus (strain MIT 9303).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9303;
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; CP000554; ABM76769.1; -; Genomic_DNA.
DR AlphaFoldDB; A2C5K9; -.
DR SMR; A2C5K9; -.
DR STRING; 59922.P9303_00121; -.
DR EnsemblBacteria; ABM76769; ABM76769; P9303_00121.
DR KEGG; pmf:P9303_00121; -.
DR HOGENOM; CLU_027272_2_3_3; -.
DR OMA; KKNPDVF; -.
DR BioCyc; PMAR59922:G1G80-13-MON; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000002274; 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_1000000520"
SQ SEQUENCE 470 AA; 51974 MW; 8249D027D34D1E4B CRC64;
MAGGVTGGSA EGWSKRFEEG LHPVIERFNA SISFDITLLQ EDLDGSIAHA RMLGECGVIS
LEEAAQLEGG LEKIRSEAAA GEFQPGLVDE DVHFAVERRL IALLGPVGKK LHTGRSRNDQ
VGTDLRLWLR RRLDDLDCEL ERFQNALLTQ AESHRQTLIP GYTHLQRAQP LCLAHHLLAY
IEMIQRDRDR LKDVRGRVNI SPLGAAALAG TSVPIDRQNT AAALGFECIY ANSLDAVSDR
DFAVEYTAAA SLVMVHLSRL AEEVIFWASE EFAFVRLSDR CATGSSLMPQ KKNPDVPELV
RGKCGRVFGH LQGLLTMIKG LPLAYNKDFQ EDKEALFDTV RTTKDCVEAM SILMEQGLEF
CSERLAAAVE SDFSNATDVA DYLVAKGVPF REAYQLVGAV VKRCLDEGIL LCDLSLEQWQ
EFHSAIAEDL HEALAPKRVV AVRISEGGTG FDRVEEQLRH WRSRLDSGVS
