ID L8J8Z5_9GAMM Unreviewed; 625 AA.
AC L8J8Z5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=C942_03026 {ECO:0000313|EMBL:ELR63947.1};
OS Photobacterium marinum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=1056511 {ECO:0000313|EMBL:ELR63947.1, ECO:0000313|Proteomes:UP000011134};
RN [1] {ECO:0000313|EMBL:ELR63947.1, ECO:0000313|Proteomes:UP000011134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK15 {ECO:0000313|EMBL:ELR63947.1,
RC ECO:0000313|Proteomes:UP000011134};
RA Khatri I., Vaidya B., Srinivas T.N.R., Subramanian S., Pinnaka A.;
RT "Genome Assembly of Photobacterium sp. AK15.";
RL Submitted (DEC-2012) 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 ECO:0000256|PIRNR:PIRNR036456}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006,
CC ECO:0000256|PIRNR:PIRNR036456}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00006}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the lyase 1 family.
CC Argininosuccinate lyase subfamily. {ECO:0000256|ARBA:ARBA00005552,
CC ECO:0000256|PIRNR:PIRNR036456}.
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:ELR63947.1}.
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DR EMBL; AMZO01000033; ELR63947.1; -; Genomic_DNA.
DR RefSeq; WP_007469307.1; NZ_AMZO01000033.1.
DR AlphaFoldDB; L8J8Z5; -.
DR PATRIC; fig|1056511.3.peg.3950; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000011134; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:UniProtKB-UniRule.
DR CDD; cd01359; Argininosuccinate_lyase; 1.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 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; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR029419; Arg_succ_lyase_C.
DR InterPro; IPR009049; Argininosuccinate_lyase.
DR InterPro; IPR011244; ASAL_AGS_AcTrfase.
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; IPR000182; GNAT_dom.
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; PF00583; Acetyltransf_1; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PIRSF; PIRSF036456; ASAL_AGS; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|PIRNR:PIRNR036456};
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006,
KW ECO:0000256|PIRNR:PIRNR036456};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_00006};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000256|PIRNR:PIRNR036456};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000256|PIRNR:PIRNR036456};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036456}.
FT DOMAIN 464..614
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 625 AA; 69678 MW; 75EA6C276BB4E29D CRC64;
MALWGGRFSQ AADTRFKQFN DSLRFDYRLA EQDIVGSIAW SKALRQVGVL TEEEQQKLEL
ALNELKLAVM EDPQQILQSD AEDIHSWVEQ QLISKVGDLG KKLHTGRSRN DQVATDLKLW
CRQQGQQLLL MLDKLQNQLV TVARDHQGTV LPGYTHLQRA QPVTFAHWCL AYVEMFERDY
SRLQDALHRL DTCPLGSGAL AGTAYPIDRE MLAHSLGFHR ATRNSLDSVS DRDHVMELLS
TASISMLHLS RMAEDLIFYN SGESNFIELA DTVTSGSSLM PQKKNPDALE LIRGKCGRVY
GAMTGMMMTV KALPLAYNKD MQEDKEGLFD ALDSWNDCME MAALCFDGIK VNKDRTLEAA
MQGYSNATEL ADYLVAKGIP FREAHHIVGV AVVAAIDKGC ALEELSLEEM KAFSPVIDED
VYAILTIDSC LEKRCALGGV APNQVDYAIG QAEKRLEKRY SPGVKVRGAR LTDLDAIEGM
VAYWAGLGEN LPRMRNELVR DIGSFAVAEH HGTVTGCASL YVYDSGLAEI RSLGVEAGWQ
HQGQGKAIVD HLIEKADQMA IKTVFVLTRV PEFFMKQGFT PTSKSLLPEK VMKDCERCPR
QHACDEVALE VRLDQEQQIR VVNVA
//
