ARLY_CERS4
ID ARLY_CERS4 Reviewed; 471 AA.
AC Q3IZY2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=RHOS4_23340;
GN ORFNames=RSP_0726;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) 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}.
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DR EMBL; CP000143; ABA79902.1; -; Genomic_DNA.
DR RefSeq; WP_011338440.1; NZ_CP030271.1.
DR RefSeq; YP_353803.1; NC_007493.2.
DR AlphaFoldDB; Q3IZY2; -.
DR SMR; Q3IZY2; -.
DR STRING; 272943.RSP_0726; -.
DR EnsemblBacteria; ABA79902; ABA79902; RSP_0726.
DR KEGG; rsp:RSP_0726; -.
DR PATRIC; fig|272943.9.peg.2679; -.
DR eggNOG; COG0165; Bacteria.
DR OMA; KKNPDVF; -.
DR PhylomeDB; Q3IZY2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000002703; Chromosome 1.
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; 1.10.275.10; -; 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 PANTHER; PTHR43814; PTHR43814; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR00838; argH; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase;
KW Reference proteome.
FT CHAIN 1..471
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000240760"
SQ SEQUENCE 471 AA; 50905 MW; 913D785CD21C89A1 CRC64;
MSDAPDPSSA ANTMWGGRFA AGPDAIMQAI NASIGFDKRL YAQDIRGSRA HAAMLAAQGI
LTSRDAEAIG EGLLTVLSEI EAGGFPFRVE LEDIHMNVEA RLKELIGEPA GRLHTARSRN
DQVAVDFRLW VRDQCDAAIS GIEALMRAFL AQAEAGADWV MPGFTHLQTA QPVTWGHHML
AYVEMLARDR SRFVDARARM NECPLGAAAL AGTGFPIDRH MTAAALGFDR PTANSLDSVS
DRDFALEFLS ASAICALHLS RFAEELVIWS SAQFRFVRLS DRWTTGSSIM PQKKNPDAAE
LLRAKMGRVL GAAVALFTVM KGLPLTYSKD MQEDKEQVFD AADTLMLGLA AMTGMVGDMQ
ANRESLAAAA ASGFSTATDL ADWLVRELNL PFRDAHHVTG TLVARAEARG CDLPDLSLAE
MQEVHPGIRE DVFAVLGVEN SVRSRTSYGG TAPDNVRAQA ARWKELLGDA A