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Database: UniProt
Entry: H8MPE0_CORCM
LinkDB: H8MPE0_CORCM
Original site: H8MPE0_CORCM 
ID   H8MPE0_CORCM            Unreviewed;       449 AA.
AC   H8MPE0;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
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   ECO:0000313|EMBL:AFE08084.1};
GN   OrderedLocusNames=COCOR_02387 {ECO:0000313|EMBL:AFE08084.1};
OS   Corallococcus coralloides (strain ATCC 25202 / DSM 2259 / NBRC 100086 / M2)
OS   (Myxococcus coralloides).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Corallococcus.
OX   NCBI_TaxID=1144275 {ECO:0000313|EMBL:AFE08084.1, ECO:0000313|Proteomes:UP000007587};
RN   [1] {ECO:0000313|EMBL:AFE08084.1, ECO:0000313|Proteomes:UP000007587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC   {ECO:0000313|Proteomes:UP000007587};
RX   PubMed=22582372; DOI=10.1128/JB.00397-12;
RA   Huntley S., Zhang Y., Treuner-Lange A., Kneip S., Sensen C.W.,
RA   Sogaard-Andersen L.;
RT   "Complete Genome Sequence of the Fruiting Myxobacterium Corallococcus
RT   coralloides DSM 2259.";
RL   J. Bacteriol. 194:3012-3013(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC   {ECO:0000313|Proteomes:UP000007587};
RA   Huntley S., Zhang Y., Treuner-Lange A., Sensen C.W., Sogaard-Andersen L.;
RT   "Genome sequence of the fruiting myxobacterium Corallococcus coralloides
RT   DSM 2259.";
RL   Submitted (MAR-2012) 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;
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; CP003389; AFE08084.1; -; Genomic_DNA.
DR   AlphaFoldDB; H8MPE0; -.
DR   STRING; 1144275.COCOR_02387; -.
DR   KEGG; ccx:COCOR_02387; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_0_7; -.
DR   InParanoid; H8MPE0; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000007587; 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; 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; 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:AFE08084.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007587}.
FT   DOMAIN          35..303
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
SQ   SEQUENCE   449 AA;  48639 MW;  3C67B2C195F98192 CRC64;
     MAETLWGKGQ PLDAAIHAFT VGDDPVVDLS LVPHDALGSA AHARMLAHVG LLAPEAATSL
     VSALHALHDE ARAGRFTIRP EQEDGHTALE AALVERTGEA GKRIHLARSR NDQVLLALRL
     FMREELLALG ARTAELAGTF LDFAEAHADL PLPGYTHLRR AMPSTFGLWG MAFAEGLLEE
     LEALKGVWGR LDRCPLGAAA GFGVPLPIDR EYVARLLGFS RVQRSPIDAQ DSRGRHEAAL
     LTWACSVAGT LEKWLWDVQL YSMDEFGFLA LPDAFTTGSS IMPQKKNPDV VELARGRCRE
     LRGLAHQVEA VAGGLPSSYH RDFQLLKRPT LQALTSAKAL LEVLSRLVPA LKVNAEKARA
     ACDDTLYAAH HAYALVAKGQ PFRDAYREVG RQLNDGSFQP DRGALTATHL GGAGNLGLAT
     AREELADARD WLTRTHAQQA QAASRVWAP
//
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