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Database: UniProt
Entry: U3GY03_9CORY
LinkDB: U3GY03_9CORY
Original site: U3GY03_9CORY 
ID   U3GY03_9CORY            Unreviewed;       485 AA.
AC   U3GY03;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
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   ORFNames=CARG_04390 {ECO:0000313|EMBL:AGU15021.1};
OS   Corynebacterium argentoratense DSM 44202.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1348662 {ECO:0000313|EMBL:AGU15021.1, ECO:0000313|Proteomes:UP000016943};
RN   [1] {ECO:0000313|EMBL:AGU15021.1, ECO:0000313|Proteomes:UP000016943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44202 {ECO:0000313|EMBL:AGU15021.1};
RX   PubMed=24092787;
RA   Bomholt C., Glaub A., Gravermann K., Albersmeier A., Brinkrolf K.,
RA   Ruckert C., Tauch A.;
RT   "Whole-Genome Sequence of the Clinical Strain Corynebacterium
RT   argentoratense DSM 44202, Isolated from a Human Throat Specimen.";
RL   Genome Announc. 1:e00793-13(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;
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; CP006365; AGU15021.1; -; Genomic_DNA.
DR   RefSeq; WP_020976174.1; NC_022198.1.
DR   AlphaFoldDB; U3GY03; -.
DR   STRING; 1348662.CARG_04390; -.
DR   GeneID; 78249674; -.
DR   KEGG; caz:CARG_04390; -.
DR   PATRIC; fig|1348662.3.peg.863; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_2_11; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000016943; 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|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:AGU15021.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016943}.
FT   DOMAIN          23..318
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          381..449
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
FT   REGION          450..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   485 AA;  51957 MW;  F472DD9942CFA83D CRC64;
     MSEVNAENNP AAHGTNQGAL WGGRFSGGPS EAMFALSVST HFDWVLAPYD VLASKAHAKV
     LNRAGLLSDG DLEAMLDGLT TLGERVASGQ FVPEPTDEDV HGAMERGLID IVGPELGGRL
     RAGRSRNDQV ATLFRMWVRD AVRDIAADVS DLVDALAAQA AAHPDAIMPG KTHSQAAQPV
     LLAHQLLAHA QPLLRDIERL RDLDKRLAVS PYGSGALAGS SLKLDPEAIA AELGFDAACD
     NSIDGTSSRD FASETAFVLA QIAVDMSRLA EEIIYWCTPE YGYVTLDDAW STGSSIMPQK
     KNPDVAELTR GKTGRLIGNL AGLMATLKAQ PLAYNRDLQE DKEPIVDSVA QLGLLLPAMT
     GLVSTLVFHT DRMHELAPAG FTLATDLAEW MVRQGVPFRE AHEASGACVR LAESRGCTLN
     ELTDEDFAMV DPRLTPSVRE VLTVEGAVAS RSTRGGTAGP RVAEQRQRVE AASAEHRRWA
     TTPVR
//
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