ARLY_BACFN
ID ARLY_BACFN Reviewed; 447 AA.
AC Q5LI10;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
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=BF0457;
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
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; CR626927; CAH06218.1; -; Genomic_DNA.
DR RefSeq; WP_010992049.1; NC_003228.3.
DR AlphaFoldDB; Q5LI10; -.
DR SMR; Q5LI10; -.
DR STRING; 272559.BF9343_0439; -.
DR EnsemblBacteria; CAH06218; CAH06218; BF9343_0439.
DR KEGG; bfs:BF9343_0439; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_0_10; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 751464at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000006731; 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; 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..447
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000116307"
SQ SEQUENCE 447 AA; 50795 MW; E4F440E8F6CAB31E CRC64;
MAQKLWEKSV EVNKDIERFT VGRDREMDLY LAKHDVLGSM AHITMLESIG LLTKEELAQL
LTELKDIYAS AERGEFVIEE GVEDVHSQVE LMLTRRLGDV GKKIHSGRSR NDQVLLDLKL
FTRTQIREVA EAVEQLFHVL IRQSERYKNV LMPGYTHLQI AMPSSFGLWF GAYAESLVDD
MLFLQAAFKM CNKNPLGSAA GYGSSFPLNR TMTTELLGFD SLNYNVVYAQ MGRGKMERNV
AFALATLAGT ISKLAFDACI FNSQNFGFVK LPDECTTGSS IMPHKKNPDV FELTRAKCNK
LQSLPQQIMM IANNLPSGYF RDLQIIKEVF LPAFQELKDC LQMTTYIMNE IKVNEHILDD
DKYLFIFSVE EVNRLAREGM PFRDAYKKVG LDIEAGHFSH DKQVHHTHEG SIGNLCNDEI
SALMQRTIEG FNFQGMEQAE KTLLGRK