ID A0A1M6LS38_MALRU Unreviewed; 455 AA.
AC A0A1M6LS38;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN02745165_03065 {ECO:0000313|EMBL:SHJ74000.1};
OS Malonomonas rubra DSM 5091.
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Geopsychrobacteraceae; Malonomonas.
OX NCBI_TaxID=1122189 {ECO:0000313|EMBL:SHJ74000.1, ECO:0000313|Proteomes:UP000184171};
RN [1] {ECO:0000313|EMBL:SHJ74000.1, ECO:0000313|Proteomes:UP000184171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5091 {ECO:0000313|EMBL:SHJ74000.1,
RC ECO:0000313|Proteomes:UP000184171};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQZT01000014; SHJ74000.1; -; Genomic_DNA.
DR RefSeq; WP_072909612.1; NZ_FQZT01000014.1.
DR AlphaFoldDB; A0A1M6LS38; -.
DR STRING; 1122189.SAMN02745165_03065; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000184171; 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|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:SHJ74000.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184171}.
FT DOMAIN 7..301
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 364..432
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 455 AA; 51239 MW; BF036B5C35332C1D CRC64;
MSKLWGGRFT QPTDKFVEEF TASIEFDQRL YAYDIQGSKA HAEMLGRQDI IAVEEANQII
AGLNDILKDI EAGKVEFSVE LEDIHMNIEA RLIERIGAVG GKLHTGRSRN DQVAVDIRLY
LRDEIDTILD YLAKLEAALI KQAEENLDVI MPGYTHLQTA QPVLYAHHML AYREMIARDI
SRLQDLRVRF NVMPLGAGAL AGTTFNIDRE WVAETLGFDG VTRNSLDSVS DRDFAIEFCS
FSSILMMHLS RLSEELILWS SADFNFIELT DAFCTGSSIM PQKKNPDVPE LVRGKTGRVY
GNLMSMLTLM KSLPLAYNKD MQEDKEPLFD TLDTVKGSLK IFADMIAEMK VKGDNMRIAA
ARGFSTATDV ADYCVRKGLP FRQAHEVVGK TVRFCVENGK DIPELTLDEF KEFSELIEED
IYDYVTLEAS VNARKATGGT AREAVERELA QLKNR
//
