ARLY_CERS5
ID ARLY_CERS5 Reviewed; 471 AA.
AC A4WVB9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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};
GN OrderedLocusNames=Rsph17025_2445;
OS Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=349102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17025 / ATH 2.4.3;
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 Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M.,
RA Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025.";
RL Submitted (APR-2007) 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; CP000661; ABP71333.1; -; Genomic_DNA.
DR AlphaFoldDB; A4WVB9; -.
DR SMR; A4WVB9; -.
DR STRING; 349102.Rsph17025_2445; -.
DR EnsemblBacteria; ABP71333; ABP71333; Rsph17025_2445.
DR KEGG; rsq:Rsph17025_2445; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_5; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 751464at2; -.
DR BioCyc; RSPH349102:G1G8M-2520-MON; -.
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; 1.10.275.10; -; 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.
FT CHAIN 1..471
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000000533"
SQ SEQUENCE 471 AA; 50632 MW; 397790774C145CA3 CRC64;
MSDAPVSSSA ANAMWGGRFA AGPDAIMQAI NASIGFDKRL YAQDIRGSRA HAAMLAAQGI
LSSRDAEAIG EGLLTVLSEI EAGGFPFRVG LEDIHMNVEA RLKELIGEPA GRLHTARSRN
DQVAVDFRLW VRDQCDAAIT GIEALMQAFV AQAEAGADWV MPGFTHLQTA QPVTWGHHML
AYVEMLARDR SRFADARARM NECPLGAAAL AGTGFPIDRH MTAAALGFDR PTANSLDSVS
DRDFALEFLS ASAICALHLS RFAEELVIWS SAQFRFVRLS DRWTTGSSIM PQKKNPDAAE
LLRAKLGRVL GAAVALFTVM KGLPLTYSKD MQEDKEQVFD AADTLMLGLA AMTGMVADMQ
ANRESLAAAA ASGFSTATDL ADWLVRELDL PFRDAHHVTG TLVARAEARG CDLPDLTLAE
MQEVHPGIRE DVFAVLGVAN SVRSRTSYGG TAPDNVRAQA ARWKELLGGT A