ID A0A0C1N5D3_9CYAN Unreviewed; 464 AA.
AC A0A0C1N5D3;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 43.
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:KAF3888810.1};
GN ORFNames=DA73_0242440 {ECO:0000313|EMBL:KIE07686.1}, DA73_0400027500
GN {ECO:0000313|EMBL:KAF3888810.1};
OS Tolypothrix bouteillei VB521301.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE07686.1};
RN [1] {ECO:0000313|EMBL:KIE07686.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KIE07686.1};
RX PubMed=25700407;
RA Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA Adhikary S.P., Tripathy S.;
RT "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL Genome Announc. 3:e00001-15(2015).
RN [2] {ECO:0000313|EMBL:KAF3888810.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KAF3888810.1};
RA Sarangi A.N., Mukherjee M., Ghosh S., Singh D., Das A., Kant S., Prusty A.,
RA Tripathy S.;
RT "Improved Assembly of Tolypothrix boutellei genome.";
RL Submitted (NOV-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}.
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:KIE07686.1}.
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DR EMBL; JHEG04000001; KAF3888810.1; -; Genomic_DNA.
DR EMBL; JHEG02000059; KIE07686.1; -; Genomic_DNA.
DR RefSeq; WP_038082978.1; NZ_JHEG04000001.1.
DR AlphaFoldDB; A0A0C1N5D3; -.
DR STRING; 1479485.DA73_0242440; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000029738; Unassembled WGS sequence.
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:KIE07686.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029738}.
FT DOMAIN 10..303
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 367..435
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 464 AA; 51990 MW; 934FBA50B300BC73 CRC64;
MAAQNTWSQR FESALHPAIA RFNASINFDI QLLEYDLMGS KAHAQMLAHT GILSRDEGEQ
LVKALDKIHE EYQQGNFNPG IEAEDVHFAV ERRLVEMVGD LGKKLHTARS RNDQVGTDTR
LYLRDRIQQI SDQLCEFQNV LLDIAEQHIE TLIPGYTHLQ RAQPLSLAHH LLAYFHMAQR
DRERLKDVSR RVNVSPLGCG ALAGTTFPID RQYTANLLKF DGIYANSLDG VSDRDFAIEF
LSAASIIMVH LSRLSEEVIL WASEEFSFVT LKDSCATGSS IMPQKKNPDV PELVRGKTGR
VFGHLQAMLV IMKGLPLAYN KDLQEDKEAL FDSVNTVTAC LEAMTILLRE GLEFRTQRLA
EAVTEDFSNA TDVADYLAAR GVPFREAYNL VGKVVKTSIA AGKLLKDLRL EEWKELHPAF
DADIYDAISP RQVVAARNSY GGTGFEQVRQ ALKAARSQTP NSDR
//
