ID A0A0M4MD07_9ACTN Unreviewed; 482 AA.
AC A0A0M4MD07;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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:VHO01715.1};
GN ORFNames=AL705_08145 {ECO:0000313|EMBL:ALE19496.1}, LC603019_01640
GN {ECO:0000313|EMBL:VHO01715.1};
OS Lawsonella clevelandensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Lawsonellaceae;
OC Lawsonella.
OX NCBI_TaxID=1528099 {ECO:0000313|EMBL:ALE19496.1, ECO:0000313|Proteomes:UP000068137};
RN [1] {ECO:0000313|EMBL:ALE19496.1, ECO:0000313|Proteomes:UP000068137}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X1698 {ECO:0000313|EMBL:ALE19496.1,
RC ECO:0000313|Proteomes:UP000068137};
RX PubMed=26659691;
RA Nicholson A.C., Bell M., Humrighouse B.W., McQuiston J.R.;
RT "Complete Genome Sequences for Two Strains of a Novel Fastidious, Partially
RT Acid-Fast, Gram-Positive Corynebacterineae Bacterium, Derived from Human
RT Clinical Samples.";
RL Genome Announc. 3:e01462-15(2015).
RN [2] {ECO:0000313|EMBL:ALE19496.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=X1698 {ECO:0000313|EMBL:ALE19496.1};
RX PubMed=27130323; DOI=10.1099/ijsem.0.001122;
RA Bell M.E., Bernard K.A., Harrington S.M., Patel N.B., Tucker T.A.,
RA Metcalfe M.G., McQuiston J.R.;
RT "Lawsonella clevelandensis gen. nov., sp. nov., a new member of the
RT suborder Corynebacterineae isolated from human abscesses.";
RL Int. J. Syst. Evol. Microbiol. 66:2929-2935(2016).
RN [3] {ECO:0000313|EMBL:VHO01715.1, ECO:0000313|Proteomes:UP000324288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USB-603019 {ECO:0000313|EMBL:VHO01715.1};
RA Seth-Smith MB H., Seth-Smith H.;
RL Submitted (APR-2019) 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; CP012390; ALE19496.1; -; Genomic_DNA.
DR EMBL; LR584267; VHO01715.1; -; Genomic_DNA.
DR RefSeq; WP_053962584.1; NZ_LR584267.1.
DR AlphaFoldDB; A0A0M4MD07; -.
DR STRING; 1528099.AL705_08145; -.
DR GeneID; 84895512; -.
DR KEGG; cbq:AL705_08145; -.
DR PATRIC; fig|1528099.3.peg.1607; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000068137; Chromosome.
DR Proteomes; UP000324288; Chromosome 1.
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:ALE19496.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000068137}.
FT DOMAIN 17..312
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 375..443
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 482 AA; 51942 MW; AE59ED48866E5EEF CRC64;
MSSSPRHETN KGSLWGGRFA DEPAQAMALL SKSTQFDWVL APYDIRASKA HARVLNRAQL
LSDEDLATML AGLDQLAADV ASGTFQPADD DEDVHGALER GLIERVGLQV GGRLRAGRSR
NDQVATLFRM WVRDALRRVG VEVLGLADAL VAQADAHMGV IMPGKTHFQA AQPVLLSHQL
LAHVHPLLRD IDRLKDLDRR TAVSPYGGGA LAGSTLDLDP EAIAAELGFA DASDNSLDGT
ASRDFVSEFA YVLAQIAVDV SRLAEEIIAW STPEFSYVTL ADAWSTGSSI MPQKKNPDVA
ELARGKAGRL IGNLSGLLAT FKALPLAYDR DLQEDKEPVF DSVAQLEMTL PAMAGLVRTL
VFHEDRMREL APRGFTLATD IAEWMVKQGV PFRQAHEAAG GCVQVAEQRG VELADLTDAE
FASVDPALTP EVRSVLTIEG SVASRKTRGG TAEPRVREQL ERVRAAIAAD VAFVESPTVP
AE
//
