ARLY_METST
ID ARLY_METST Reviewed; 465 AA.
AC Q2NGN7;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 95.
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=Msp_0618;
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
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; CP000102; ABC57016.1; -; Genomic_DNA.
DR RefSeq; WP_011406216.1; NC_007681.1.
DR AlphaFoldDB; Q2NGN7; -.
DR SMR; Q2NGN7; -.
DR STRING; 339860.Msp_0618; -.
DR EnsemblBacteria; ABC57016; ABC57016; Msp_0618.
DR GeneID; 41325194; -.
DR KEGG; mst:Msp_0618; -.
DR eggNOG; arCOG01748; Archaea.
DR HOGENOM; CLU_027272_2_3_2; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 51806at2157; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001931; 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..465
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000240791"
SQ SEQUENCE 465 AA; 52209 MW; A48E83EBDCB8B668 CRC64;
MDLRAGRFDG QMTDDAAQFS SSIEFDKRIF KSDIKCNRAH TTMLIEEGII PKESGKKILK
ALDKLEKEGI GALNLDPSFE DIHMALEDYV TKEIGDEAGF MHTAKSRNDQ VCTDIRLTLK
EEIENTISNI KSFIKTIVEM AKENTHTLFI AYTHLQHAQP TTFAHHLMAY ANELRRDCER
LIDTYKRVDM NPLGSAALTT TGFPINRERT TELLGFSKVM DNSIDGVSSR DFAAEAIFDY
AMLSTTLGKI SDEIVIWSSY EFRMVECSNQ YSSTSSIMPQ KKNPDIAELS RGKSTIAYGE
LMTVLSMIKG IPHSYNRDLQ EVTPHLWNAI DNTNDILRIV HGMLSTLTIN KDRTEELAGA
NFATATELAD VMVREKNLPF RTAHRIVGRV VSEAIDDNIT THDIDNDYVN RVSVEVMGKP
INLGEDLVKQ ALNPLRNVKS RTVIGGCAPE AVNDAIEKME IFLNE