ID ARLY_RHOPB Reviewed; 465 AA.
AC Q20WT9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 24-JAN-2024, entry version 96.
DE RecName: Full=Argininosuccinate lyase {ECO:0000255|HAMAP-Rule:MF_00006};
DE Short=ASAL {ECO:0000255|HAMAP-Rule:MF_00006};
DE EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006};
DE AltName: Full=Arginosuccinase {ECO:0000255|HAMAP-Rule:MF_00006};
GN Name=argH {ECO:0000255|HAMAP-Rule:MF_00006}; OrderedLocusNames=RPC_4875;
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-2006) 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; Evidence={ECO:0000255|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. {ECO:0000255|HAMAP-
CC Rule:MF_00006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00006}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00006}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD90397.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000301; ABD90397.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q20WT9; -.
DR SMR; Q20WT9; -.
DR STRING; 316056.RPC_4875; -.
DR KEGG; rpc:RPC_4875; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_5; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
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; Arginine biosynthesis; Cytoplasm; Lyase.
FT CHAIN 1..465
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000240762"
SQ SEQUENCE 465 AA; 50413 MW; DD49CFDDC41CC2AD CRC64;
MSNKMWGGRF SERPDAIMEE INVSIDVDRH LYAQDIAASK AHAAMLAAQG IVTAKDAKNI
AKGLDTILSE IVAGSFDFKR ALEDIHMNVE SRLSELIGPA AGRLHTARSR NDQVATDFRL
FVRDTIDGID AALASYQHAL ATRALEHADT VMPGFTHLQT AQPVTFGHHL MAYVEMAARD
RGRFRDARKR LNESPLGAAA LAGTSFPIDR DATAKALGFE RPMANSLDAV SDRDFVLETL
AAASIAAVHL SRFAEEIVLW TSPLVGMVRL SDKFTTGSSI MPQKRNPDAA ELARAKTGRV
IGALTGLLIV MKGLPLAYQK DMQEDKQGAM EAFAALSLAI RAMSGMVSDL VPDPARMKQA
AGEGYATATD LADWLVRELK MPFRDAHHVT GRIVGEASKQ GVALHELPLA EMQAIEPRIT
QQALSVLSVE SSVKSRVSYG GTAPKNVRAQ AKAWLKRLEK EHNSG
//
