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Database: UniProt
Entry: H8GVE2_DEIGI
LinkDB: H8GVE2_DEIGI
Original site: H8GVE2_DEIGI 
ID   H8GVE2_DEIGI            Unreviewed;       436 AA.
AC   H8GVE2;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=Argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE            Short=ASAL {ECO:0000256|HAMAP-Rule:MF_00006};
DE            EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338, 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   OrderedLocusNames=DGo_CA0392 {ECO:0000313|EMBL:AFD24319.1};
OS   Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD24319.1, ECO:0000313|Proteomes:UP000007575};
RN   [1] {ECO:0000313|EMBL:AFD24319.1, ECO:0000313|Proteomes:UP000007575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0
RC   {ECO:0000313|Proteomes:UP000007575};
RX   PubMed=22470573; DOI=10.1371/journal.pone.0034458;
RA   Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R.,
RA   Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S., Wang Y.,
RA   Lin M.;
RT   "Genome sequence and transcriptome analysis of the radioresistant bacterium
RT   Deinococcus gobiensis: insights into the extreme environmental
RT   adaptations.";
RL   PLoS ONE 7:E34458-E34458(2012).
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000985, 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.
CC       {ECO:0000256|ARBA:ARBA00004941, ECO:0000256|HAMAP-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}.
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DR   EMBL; CP002191; AFD24319.1; -; Genomic_DNA.
DR   AlphaFoldDB; H8GVE2; -.
DR   STRING; 745776.DGo_CA0392; -.
DR   KEGG; dgo:DGo_CA0392; -.
DR   PATRIC; fig|745776.4.peg.399; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_0; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000007575; 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; 1.10.40.30; 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; IPR020557; Fumarate_lyase_CS.
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.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW   Rule:MF_00006}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000313|EMBL:AFD24319.1}.
FT   DOMAIN          3..280
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          343..410
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   436 AA;  47489 MW;  3A6BD06B6FB5AE79 CRC64;
     MGFDQRLAEQ DIRGSLAHVA MLGQVGILSA EEVAQITGGL NAVLADIRTG AFEWRLDRED
     VHMNVEAALR DRIGPVAGKL HTARSRNDQV AVDFRLFTKE AALDLADKTR ALRTVMLDEA
     EKHLETGVIL PGYTHLQVAQ PILLAHWFMA YVAMLERDEG RFRDAAERMD ESPLGSSALA
     GTPWPIDRFA TAGALGFARP TANSLDGVGS RDFAIEFLSA CAILSAHLSR LSEELILYST
     FEFGFLTLPD SHTTGSSIMP QKKNPDVSEL ARGKAGRVFG NLMGLLTVVK GTPLAYNKDL
     QEDKEGVFDS YDTLSIVLRL YAEMMPKTVW HAEKTREAAA RGYSTATDVA DFLARQGVPF
     REAHEVVGGL VGLASRSGRQ LWELSDAELK AAHPLLSAEV AQTLTVEESV RGRQSYGGTA
     PEQVARAIAD AKRALE
//
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