ARLY_METBU
ID ARLY_METBU Reviewed; 491 AA.
AC Q12X66;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=Mbur_1025;
OS Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS ACE-M).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=259564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z., Ting L.,
RA Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J., Ivanova N.,
RA Dalin E., Martinez M., Lapidus A., Hauser L., Land M., Thomas T.,
RA Cavicchioli R.;
RT "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT burtonii: the role of genome evolution in cold adaptation.";
RL ISME J. 3:1012-1035(2009).
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; CP000300; ABE51960.1; -; Genomic_DNA.
DR RefSeq; WP_011499109.1; NC_007955.1.
DR AlphaFoldDB; Q12X66; -.
DR SMR; Q12X66; -.
DR STRING; 259564.Mbur_1025; -.
DR EnsemblBacteria; ABE51960; ABE51960; Mbur_1025.
DR GeneID; 3998128; -.
DR KEGG; mbu:Mbur_1025; -.
DR HOGENOM; CLU_027272_2_3_2; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 51806at2157; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001979; 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; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase;
KW Reference proteome.
FT CHAIN 1..491
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000000498"
SQ SEQUENCE 491 AA; 54140 MW; 79B8AA286C870CC6 CRC64;
MSDILRRGRL ASVPDEEIIN FTSSMNADKW IFKADILVDL AHTIMLKERK IIKAEDCKKI
LEGLLTIKEE GIEKLDHTYE DIHISLESRL IDMVGEDTGG RMHSGRSRND EVATCIRLTL
RNDLLLLMEE LIALRNTLND TSSENLNTLM PGFTHLQHAQ PTTLAHHLTA HANAIGRDLE
RTMDCYKRVN LSPLGAAAFA STGFDLDRER TCKLLGFDGL IENSMDAVSS RDFLIESASV
FANLMINLSK VAEEIVIWST SEFAFIELDD RYASTSSIMP QKKNPDTAEL LRGKSGVTIG
SLMSLLAICK ALPLSYNRDL QEATPNIMQS LETTRASVRI MNGMIATMSI NKENMAGLAT
AGFTTATELA DTMVRVCDIP FRTAHQIVGV LARGSGEPTL GEIDAVAHNV IGESLSSRGL
TEKMVKEALD PILNVSKRSV IGGPSPESME RLIESSRERI ANNTEILESL IANRDNAIES
LFCEVEKCID V