ARLY_METVS
ID ARLY_METVS Reviewed; 481 AA.
AC A6URI4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
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=Mevan_1208;
OS Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS / SB).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=406327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus vannielii SB.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000742; ABR55106.1; -; Genomic_DNA.
DR RefSeq; WP_012066021.1; NC_009634.1.
DR AlphaFoldDB; A6URI4; -.
DR SMR; A6URI4; -.
DR STRING; 406327.Mevan_1208; -.
DR EnsemblBacteria; ABR55106; ABR55106; Mevan_1208.
DR GeneID; 5325684; -.
DR KEGG; mvn:Mevan_1208; -.
DR eggNOG; arCOG01748; Archaea.
DR HOGENOM; CLU_027272_2_3_2; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 51806at2157; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001107; 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.
FT CHAIN 1..481
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000000503"
SQ SEQUENCE 481 AA; 54254 MW; B22A4BD34E26BE83 CRC64;
MNILRRGRLG SSVKEDVMKF TTSLEFDKEI FQSDILCDIA HTTMLMEQKI VSIEFGEKVI
EELKKIAKVG MDSLNLDPSL DDIHMVIESE LIKKLGEDVA GRMHTGRSRN DEVATDLRLS
LRKKVLEIVK LLIDMEENML SLAKEHSETI TVGYTHLQQA QPVTFGHQIL SHVSAVERDI
SRFFDAYNRI NISPLGCGAM ATTGFNIDRK RTMELLGFYE LIENSMDGVS SRDFIVETMA
NISMLGTNLS KICEELILFS TAEFKTVEIA DEYTSTSSIM PQKKNPDVAE IARAKLSTLN
GNLITVLTIM KALPNTYNRD LQEISPHLWK STYTIIDCIK MIDGMVSTIK VNKERMKENA
EKNYATATEL ADTLVRECNI AFRMAHGIVG ELVRTSIEEK VEIKDIILDV FKANGLHLSK
EKIDSALDPY ENVKLRDVIG GPAPKEVERA VLSFKNKMEL HSKNLNDKMR SIEAVEENLL
N