ID A0A0D3LKP1_9BACT Unreviewed; 447 AA.
AC A0A0D3LKP1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=D770_20820 {ECO:0000313|EMBL:AHM62413.1};
OS Flammeovirgaceae bacterium 311.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae.
OX NCBI_TaxID=1257021 {ECO:0000313|EMBL:AHM62413.1, ECO:0000313|Proteomes:UP000064112};
RN [1] {ECO:0000313|EMBL:AHM62413.1, ECO:0000313|Proteomes:UP000064112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=311 {ECO:0000313|EMBL:AHM62413.1,
RC ECO:0000313|Proteomes:UP000064112};
RA Fang C.;
RT "Complete bacteria genome obtained just from illumina data.";
RL Submitted (NOV-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 -!- 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; CP004371; AHM62413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D3LKP1; -.
DR STRING; 1257021.D770_20820; -.
DR KEGG; fbt:D770_20820; -.
DR PATRIC; fig|1257021.3.peg.4700; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000064112; 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; 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; 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:AHM62413.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000064112}.
FT DOMAIN 25..298
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
SQ SEQUENCE 447 AA; 50127 MW; E5D5B461666FC63E CRC64;
MKLWDKGFTV ENKIESYTVG KDRELDIHLA PYDVLGSLAH ATMLQSVGLI SEEELEQLKQ
GLQGIYQQIE RGQFTIQDGV EDVHSQVELQ LTQQLGDAGK RVHTARSRND QVLVDLKMYL
RAEVKELVGL VSGLFETLLQ AAEQHKDILI PGYTHLQAAM PSSFGLWFSA YAESLADDLR
LLYAAYGIIN QNPLGSGAGY GSSLPINRTL TTELLGFDSM HVNVVNAQLS RGKTELSLAF
AMAGISHTLS KLAMDVCLYN SQNFGFLTFP DELTTGSSIM PHKKNPDVFE LMRGKSNRQM
ALPNEIMMLT ASMPSGYHRD FQLLKEILFP ALEELKNSLG ICSYMLQRAK VNPDAIRDDK
YKYIYSVEEV NKKVMAGVPF RQAYKEVGAA INDGTYQPAL EVQHTHEGSI GNLRLDLIRQ
KFRSVQQQFS FHKWEQALEK LLMAQNA
//
