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Database: UniProt
Entry: A0A164CVJ8_9MICO
LinkDB: A0A164CVJ8_9MICO
Original site: A0A164CVJ8_9MICO 
ID   A0A164CVJ8_9MICO        Unreviewed;       480 AA.
AC   A0A164CVJ8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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:KZE92608.1};
GN   ORFNames=AVP42_02293 {ECO:0000313|EMBL:KZE92608.1};
OS   Agromyces sp. NDB4Y10.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Agromyces.
OX   NCBI_TaxID=1775951 {ECO:0000313|EMBL:KZE92608.1, ECO:0000313|Proteomes:UP000185889};
RN   [1] {ECO:0000313|EMBL:KZE92608.1, ECO:0000313|Proteomes:UP000185889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NDB4Y10 {ECO:0000313|EMBL:KZE92608.1,
RC   ECO:0000313|Proteomes:UP000185889};
RA   Adelskov J., Patel B.K.;
RT   "Draft genome sequence of Agromyces sp. NDB4Y10 isolated from a newly
RT   drilled coal seam bore well.";
RL   Submitted (JAN-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZE92608.1}.
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DR   EMBL; LQGY01000050; KZE92608.1; -; Genomic_DNA.
DR   RefSeq; WP_067949179.1; NZ_LQGY01000050.1.
DR   AlphaFoldDB; A0A164CVJ8; -.
DR   STRING; 1775951.AVP42_02293; -.
DR   PATRIC; fig|1775951.3.peg.2370; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000185889; 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; 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|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   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:KZE92608.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185889}.
FT   DOMAIN          31..313
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          376..444
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   480 AA;  51108 MW;  6741DEB1E8F0C9C5 CRC64;
     MADAHGTHGT NEGSLWGARF AAGPSPELQR LSKSTHFDWQ LAPYDLAGSR AHARALAAAG
     YLDPGELDRM LAGLDALEAR FLAGELVAAD SDEDVHGALE AALIAEVGPE LGGKLRAGRS
     RNDQIATLVR LYLKDHAATI GRQLVHLIDA LAAQADAHRT AIMPGRTHLQ HAQPVLLAHH
     LLAHGWALSR DLERLIDWLK RADVSPYGGG ALAGSTLGLD AASVARDLGL AAPAENSIDG
     TASRDVVAEF AFVAAMIGID LSRISEEVIL WNTREFGFVT LDDAYSTGSS IMPQKKNPDI
     AELARGKSGR LIGNLTGLLA TLKALPLAYN RDLQEDKEPV FDSVETLEVL LPAFTGMVET
     LTFHTDRMAE LAPAGFSLAT DVAEWLVQRH VPFRDAHEIT GALVRYAEQH GLELHEVDDA
     GLAAVSPHLT PEVRQVLTIE GSVASRDGVG GTAPVRVDAQ FAALADRVRH LVQALPGGDA
//
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