ARLY_RHOBA
ID ARLY_RHOBA Reviewed; 460 AA.
AC Q7UK64;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 25-MAY-2022, entry version 102.
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=RB10834;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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=CAD77017.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX294152; CAD77017.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_869639.1; NC_005027.1.
DR RefSeq; WP_037227775.1; NC_005027.1.
DR AlphaFoldDB; Q7UK64; -.
DR SMR; Q7UK64; -.
DR STRING; 243090.RB10834; -.
DR EnsemblBacteria; CAD77017; CAD77017; RB10834.
DR KEGG; rba:RB10834; -.
DR PATRIC; fig|243090.15.peg.5228; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_0; -.
DR InParanoid; Q7UK64; -.
DR OrthoDB; 751464at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IBA:GO_Central.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
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..460
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137814"
SQ SEQUENCE 460 AA; 51855 MW; E34639432AA7E9EB CRC64;
MASPSRSGVF QAETDARLEA YAESISFDSR LYEHDIRGSI AHANMLREVG LLTEDEFKLI
RDTLETIRGE LDRGELPMRF ELEDIHMHVE QALIDRIGDT GRKLHTARSR NDQVSTDTRM
WIRQSLDEID ALLVDLQSAF LSRCENDFDI ILPAYTHLQR AQPVLAPHYW LAYIEKLERD
RQRIADCRKR VNQCSLGIAA VAGTTLPIDR QHTASALDFE GITANSLDTS SDRDFVVEST
FVMSLIASHL SGWAEEWILW STVEFDFIQI PQAFCTGSSI MPQKVNPDTL ELTRGKSARV
MGALQTLMLL IKNLPLAYNR DLQEDKPPLF DAFDTTRAML ELAAPIVRGA ELKRESIAAR
IEKGYLDATT LMEWMIARGM PQRTAHHLVG AIVSEAMQQG VTLSDLPLET YQKLSDQIDE
SVYEVLGTSN AIAAFRSEGS TAPARVREQI KQWTSRLENA