ARLY_CUTAK
ID ARLY_CUTAK Reviewed; 468 AA.
AC Q6A816;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 25-MAY-2022, entry version 116.
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=PPA1346;
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Cutibacterium.
OX NCBI_TaxID=267747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202;
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT83099.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE017283; AAT83099.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_002531318.1; NZ_CP025935.1.
DR AlphaFoldDB; Q6A816; -.
DR SMR; Q6A816; -.
DR STRING; 267747.PPA1346; -.
DR EnsemblBacteria; AAT83099; AAT83099; PPA1346.
DR KEGG; pac:PPA1346; -.
DR PATRIC; fig|267747.3.peg.1389; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_2_11; -.
DR OMA; KKNPDVF; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000000603; 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..468
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137802"
SQ SEQUENCE 468 AA; 50470 MW; DD9BD0DCBEC919A3 CRC64;
MALWGGRFSG GPSEALAALS VSTQFDWRLA RHDIAGSSAH AGVLHAAGLL DDDQYEGMMK
ALNALEEDVV SGRFVAQPED EDVHTALERG LMERAGKDLG GRLRAGRSRN DQIIALLRRY
LREEARSLAG ELLGLAHVLS RQAEDVGDAV IAGRTHMQHA QPVLLAHQLL AHAWPLLRDV
QRFRDLDARL DCSPYGSGAL AGSSLGLDPE AVARDLGFSS SVPNSIDGTA ARDVVAEFAF
VAAQVGVDLS RLSEEIIIWN TREFGYVTLD DSFSTGSSIM PQKKNPDIAE LARGKAGRLI
GDLAGLMASL KGLPLAYARD LQEDKEPVFD QIDQLHLLLP AITGMVDTAV FNTDRMAEMA
GQGFSLATDV AEWLVRQGVP FRVAHELSGA CVRGAESQNK ELADLTDQEL IAIDPRLTPQ
VREVMTVQGS VRSRAGRGGT APERVAEQIT ELREAIAGLR SFGEAETR