ARLY_BACTN
ID ARLY_BACTN Reviewed; 446 AA.
AC Q8A1D3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=BT_3733;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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; AE015928; AAO78838.1; -; Genomic_DNA.
DR RefSeq; NP_812644.1; NC_004663.1.
DR RefSeq; WP_008766984.1; NC_004663.1.
DR AlphaFoldDB; Q8A1D3; -.
DR SMR; Q8A1D3; -.
DR STRING; 226186.BT_3733; -.
DR PaxDb; Q8A1D3; -.
DR PRIDE; Q8A1D3; -.
DR EnsemblBacteria; AAO78838; AAO78838; BT_3733.
DR GeneID; 60924902; -.
DR KEGG; bth:BT_3733; -.
DR PATRIC; fig|226186.12.peg.3794; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_0_10; -.
DR InParanoid; Q8A1D3; -.
DR OMA; KKNPDVF; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IBA:GO_Central.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR CDD; cd01359; Argininosuccinate_lyase; 1.
DR Gene3D; 1.10.275.10; -; 1.
DR HAMAP; MF_00006; Arg_succ_lyase; 1.
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; 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..446
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000116309"
SQ SEQUENCE 446 AA; 50628 MW; 59C9F2F8F953A430 CRC64;
MAQKLWEKSV QVNKDIERFT VGRDREMDLY LAKHDVLGSM AHITMLESIG LLTKEELEQL
LAELKTIYAS VERGEFIIEE GVEDVHSQVE LMLTRRLGDV GKKIHSGRSR NDQVLLDLKL
FTRTQIREIA EAVEQLFHVL ILQSERYKNV LMPGYTHLQI AMPSSFGLWF GAYAESLVDD
MQFLQAAFRM CNRNPLGSAA GYGSSFPLNR TMTTDLLGFD SLNYNVVYAQ MGRGKLERNV
AFALATIAGT ISKLAFDACM FNSQNFGFVK LPDDCTTGSS IMPHKKNPDV FELTRAKCNK
LQSLPQQIMM IANNLPSGYF RDLQIIKEVF LPAFQELKDC LQMTTYIMNE IKVNEHILDD
DKYLFIFSVE EVNRLAREGM PFRDAYKKVG LDIEAGKFTH DKQVHHTHEG SIGNLCNDEI
SALMQQVVDG FNFCGMEQAE KALLGR