ARLY_BIFLO
ID ARLY_BIFLO Reviewed; 490 AA.
AC Q8G5F3;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=BL1057;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN24865.1; -; Genomic_DNA.
DR RefSeq; NP_696229.1; NC_004307.2.
DR RefSeq; WP_007051162.1; NC_004307.2.
DR AlphaFoldDB; Q8G5F3; -.
DR SMR; Q8G5F3; -.
DR STRING; 206672.BL1057; -.
DR EnsemblBacteria; AAN24865; AAN24865; BL1057.
DR GeneID; 66504807; -.
DR KEGG; blo:BL1057; -.
DR PATRIC; fig|206672.9.peg.763; -.
DR HOGENOM; CLU_027272_2_2_11; -.
DR OMA; KKNPDVF; -.
DR PhylomeDB; Q8G5F3; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000000439; 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..490
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137741"
SQ SEQUENCE 490 AA; 53392 MW; 947BC541D5A7E78A CRC64;
MTENNEHLAL WGGRFTSGPS PELARLSKST QFDWRLADDD IAGSRAHARA LGRAGLLTAD
ELQRMEDALD TLQRHVDDGS FAPIEDDEDE ATALERGLID IAGDELGGKL RAGRSRNDQI
ACLIRMWLRR HSRVIAGLLL DLVNALIEQS EKAGRTVMPG RTHMQHAQPV LLAHQLMAHA
WPLIRDVQRL IDWDKRINAS PYGSGALAGN TLGLDPEAVA RELGFSRVTD NSIDGTAARD
LVAEFAFVAA MTGVDISRLS EEIIIWNTQE FAFVKLDDGY STGSSIMPQK KNPDIAELAR
GKSGRLIGDL TGLLATLKGL PTAYARDLQE DKEAVFDQVD TLEVLLPAFT GMVRTMHFDG
DRLEEEAPTG FALATDIAEW LVKNGVPFRH AHELSGACVK LAEGRGQELW DLTDNDFIET
FAAFLPADKA PGVREVLSSH GSVDSRNGKG GTAYGRVREQ IADAKAEVEE LKLFPASTSD
GSAYKAPGTF