ID A0A0D6AD63_9CHRO Unreviewed; 459 AA.
AC A0A0D6AD63;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=GM3708_1104 {ECO:0000313|EMBL:BAQ60698.1};
OS Geminocystis sp. NIES-3708.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Geminocystis.
OX NCBI_TaxID=1615909 {ECO:0000313|EMBL:BAQ60698.1, ECO:0000313|Proteomes:UP000060542};
RN [1] {ECO:0000313|EMBL:BAQ60698.1, ECO:0000313|Proteomes:UP000060542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3708 {ECO:0000313|EMBL:BAQ60698.1,
RC ECO:0000313|Proteomes:UP000060542};
RA Hirose Y.;
RT "Geminocystis sp. NIES-3708 complete genome sequence.";
RL Submitted (MAR-2015) 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; AP014815; BAQ60698.1; -; Genomic_DNA.
DR RefSeq; WP_066344726.1; NZ_AP014815.1.
DR AlphaFoldDB; A0A0D6AD63; -.
DR STRING; 1615909.GM3708_1104; -.
DR KEGG; gee:GM3708_1104; -.
DR PATRIC; fig|1615909.3.peg.1128; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000060542; 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|HAMAP-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:BAQ60698.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000060542}.
FT DOMAIN 10..303
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 367..434
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 459 AA; 51498 MW; DE5199018DD4DBFC CRC64;
MTKKQTWSDR FETSLHPVIA VFNASIGFDI ELIEYDLTGS IAHAKMLGYT GIITPEEAQT
LIKGLEEIRQ EYRDGNFNPG VDQEDVHFAV ERRLTEIVGD VGKKLHTGRS RNDQVGTDIR
LYLRDQIQQI QGLLRNWQQA LLNHAENHIE TLIPGYTHLQ RAQPISLAHH LMAYCQMAQR
DWERLSQIYD RTNISPLGCG ALAGTTFPID RHFSAKELGF ASVYENSLDG VSDRDFAIEF
LCASSLIMVH LSRISEELIL WASQEFSFIT LKDNCSTGSS IMPQKKNPDI PELVRGKTGR
VFGHLQGLLT IMKGLPLAYN KDLQEDKEGI FDTVDTVKGC LTAMTILLSE GLEFRISRLE
EAVNEDFSNA TDVADYLASK GVPFREAYNL VGKVVKTSLG AGKLLKDLTI EEWQQLHPAF
ETDIYQAIAP KQVVSARNSY GGTGFEQIKQ AITNLKNKM
//
