GenomeNet

Database: UniProt
Entry: V4XSM6_9ARCH
LinkDB: V4XSM6_9ARCH
Original site: V4XSM6_9ARCH 
ID   V4XSM6_9ARCH            Unreviewed;       500 AA.
AC   V4XSM6;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Argininosuccinate lyase {ECO:0000256|HAMAP-Rule:MF_00006};
DE            Short=ASAL {ECO:0000256|HAMAP-Rule:MF_00006};
DE            EC=4.3.2.1 {ECO:0000256|HAMAP-Rule:MF_00006};
DE   AltName: Full=Arginosuccinase {ECO:0000256|HAMAP-Rule:MF_00006};
GN   Name=argH {ECO:0000256|HAMAP-Rule:MF_00006};
GN   ORFNames=A07HR67_02606 {ECO:0000313|EMBL:ESS03096.1};
OS   uncultured archaeon A07HR67.
OC   Archaea; environmental samples.
OX   NCBI_TaxID=1412871 {ECO:0000313|EMBL:ESS03096.1, ECO:0000313|Proteomes:UP000030660};
RN   [1] {ECO:0000313|Proteomes:UP000030660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24335829;
RA   Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S.,
RA   Heidelberg K.B., Banfield J.F., Allen E.E.;
RT   "Seasonal fluctuations in ionic concentrations drive microbial succession
RT   in a hypersaline lake community.";
RL   ISME J. 0:0-0(2013).
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:0000256|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:0000256|HAMAP-
CC       Rule:MF_00006}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00006}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KI543168; ESS03096.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4XSM6; -.
DR   STRING; 1412871.A07HR67_02606; -.
DR   PATRIC; fig|1412871.3.peg.2754; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000030660; Unassembled WGS sequence.
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; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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   NCBIfam; TIGR00838; argH; 1.
DR   PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR   Pfam; PF14698; ASL_C2; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; ARGSUCLYASE.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000313|EMBL:ESS03096.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030660}.
FT   DOMAIN          71..308
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          371..447
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   500 AA;  51517 MW;  5E80C37DCB3B87DA CRC64;
     MTDDPSGSDD DAAAGSGTAV RRDRFSGGPA REFLSSLAAD EALFPADLAV DRAHVIMLAE
     QDIVDDGVAG DILAALADVE AAGHAALPDG EDVHEAIETA VIDRMGPDGG RMHTARSRND
     EVAACIRYRL REDLLAVAEA TVTLREALID VAKAHTETVM PGYTHLQPAQ PTTVAHYLLS
     YEGAVARDTE RLLGAYDRTN RSPLGGAAFA GTPFDIDRER TAALLGFDGV VSNSMDAASA
     RDFLAEGSTA CATLAMSLSG LAEDLILFSN KGFLELSDAY ASTSSIMPQK KNPDTLELTR
     GVAGDAIGEA TGTFSLLKGL PRAYNRDLQR AHAGVFEVAG DVREATAVAA GAVATADWAV
     ETLAETAGDG FSTATGVADL LAAAGMPFRT AHEVVAAAAE TIDDADAPAA AAATIEEAVR
     DVAGDSLSAY VSRADVEAAL DPVNSVADRD SAGGPAPDAV AEAIATAESA LDDDAAALDA
     RRDRLAAAAD RRETEVATYV
//
DBGET integrated database retrieval system