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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//