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Database: UniProt
Entry: A0A290ZJ58_9RHOO
LinkDB: A0A290ZJ58_9RHOO
Original site: A0A290ZJ58_9RHOO 
ID   A0A290ZJ58_9RHOO        Unreviewed;       473 AA.
AC   A0A290ZJ58;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
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:ATE59019.1};
GN   ORFNames=CCZ27_02745 {ECO:0000313|EMBL:ATE59019.1};
OS   Thauera sp. K11.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=2005884 {ECO:0000313|EMBL:ATE59019.1, ECO:0000313|Proteomes:UP000217984};
RN   [1] {ECO:0000313|EMBL:ATE59019.1, ECO:0000313|Proteomes:UP000217984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K11 {ECO:0000313|EMBL:ATE59019.1,
RC   ECO:0000313|Proteomes:UP000217984};
RA   Xi L., Qiao N.;
RT   "Thauera phenolivorans sp. nov., a phenol derivative-degrading bacterium
RT   isolated from activated sludge and an emended description of the genus
RT   Thauera.";
RL   Submitted (SEP-2017) 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; CP023439; ATE59019.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A290ZJ58; -.
DR   KEGG; thk:CCZ27_02745; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000217984; 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:ATE59019.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217984}.
FT   DOMAIN          18..312
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          375..449
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   473 AA;  51731 MW;  8F06CB2C460EBC11 CRC64;
     MTDTTSPGAD APAKTWSGRF TEPVSDLVKR YTASVSFDRR MAKQDIRGSL AHAKMLAKQG
     IIGAQDLADI ERGMAQIAGE IERGEFAWSL DDEDVHLNIE KRLTALVGDA GKRLHTGRSR
     NDQVATDIRL WLRDAIDRIL TLIAEFQHNL LTVAEAHAAT PMPGFTHLQV AQPVTFGHHL
     MAYYEMSRRD AERLEDCRRR VNRLPLGSAA LAGTGYPIDR EFVAAELGFD EVCRNSLDAV
     SDRDFAIEFC AASALLMTHL SRLSEELILW MSPRVGFIDL ADRFCTGSSI MPQKKNPDVP
     ELVRGKTGRV NGSLIALLTL MKGQPLAYNK DNQEDKEPLF DTADTVIDTL RIYADMITGI
     KVKPEAMRGA LSQGYATATD LADYLVKQGL PFRDAHEAVA LAVRAADVKG CDLPQFSLDE
     LRIAMAHVPG AAERVGEDVF AVLTVEGSLA SRNHVGGTAP AQVRAAIALA RRG
//
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