ID A8V155_9AQUI Unreviewed; 305 AA.
AC A8V155;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338};
DE EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338};
DE Flags: Fragment;
GN ORFNames=HG1285_09501 {ECO:0000313|EMBL:EDP73900.1};
OS Hydrogenivirga sp. 128-5-R1-1.
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Hydrogenivirga.
OX NCBI_TaxID=392423 {ECO:0000313|EMBL:EDP73900.1, ECO:0000313|Proteomes:UP000005981};
RN [1] {ECO:0000313|EMBL:EDP73900.1, ECO:0000313|Proteomes:UP000005981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=128-5-R1-1 {ECO:0000313|EMBL:EDP73900.1,
RC ECO:0000313|Proteomes:UP000005981};
RA Reysenbach A.-L., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) 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};
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}.
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:EDP73900.1}.
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DR EMBL; ABHJ01000125; EDP73900.1; -; Genomic_DNA.
DR RefSeq; WP_008288638.1; NZ_ABHJ01000125.1.
DR AlphaFoldDB; A8V155; -.
DR PATRIC; fig|392423.7.peg.1045; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000005981; Unassembled WGS sequence.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-EC.
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 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 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Lyase {ECO:0000313|EMBL:EDP73900.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005981}.
FT DOMAIN 2..149
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 211..274
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDP73900.1"
SQ SEQUENCE 305 AA; 34374 MW; 6A72C33157EDF170 CRC64;
AYTHLQRAQP IRLAHYFLAY LEMYNRDEER FKDNLKRIDQ LPLGSGALAG VDFPLDREFV
AKELGFSEIM RNSLDATASR DAVIEFLSNA SICMANLSRQ SEDLIIWNSA EFSFVELPDK
LTTGSSIMPQ KKNPDVLELI RGKVGRVYGD LVALLTIVKG LPMAYNRDLQ EDKEPVFDAV
KTLKGSIIGM TKIIEGLKPR KDIMEKAAGG FALATDLANY LVRKGLPFRQ AHHVVGQIVG
YLTQQGRELE SITLEELKKF SHLFEEDALN ILNPYYVADA RKTFGGTAKE RVLEQINYWK
EKLGA
//
