ARLY_THISH
ID ARLY_THISH Reviewed; 467 AA.
AC B8GSV2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 65.
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=Tgr7_0033;
OS Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-EbGR7;
RX PubMed=21475584; DOI=10.4056/sigs.1483693;
RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL71137.1; -; Genomic_DNA.
DR RefSeq; WP_012636626.1; NC_011901.1.
DR AlphaFoldDB; B8GSV2; -.
DR SMR; B8GSV2; -.
DR STRING; 396588.Tgr7_0033; -.
DR EnsemblBacteria; ACL71137; ACL71137; Tgr7_0033.
DR KEGG; tgr:Tgr7_0033; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_6; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 751464at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000002383; 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; 1.10.275.10; -; 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..467
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000116349"
SQ SEQUENCE 467 AA; 51761 MW; 87C47BAB2BB8159B CRC64;
MSTQHSGDKL WGGRFSEPTD AFVEAFTASV SFDQRLYRHD IQGSKAHARM LARVGVLTEE
ECDKIHDGLD AILADIERGD FAWSVELEDV HMNVEARLIE RIGDVGKKLH TGRSRNDQVA
TDIRLYLREA IDALMQEIRR LQGGLVDLAE REAQTIMPGF THLQTAQPVT FGHHMMAWYE
MLERDHGRLA DCRKRVNVLP LGAAALAGTP YPLDRHYTAE LLGFDAVTDN SLDAVSDRDF
AIEFCAAGAL IMTHLSRFSE ELILWASAQF GFVDLPDRFC TGSSIMPQKK NPDVPELVRG
KTGRANGNLI ALLTLMKGQP LAYNKDNQED KEPLFDTVDT LAGSLRAFAD MVPHIQVRAE
VMRAAASRGF ATATDLADYL VRRGMPFRDA HEVVGRAVRH GVETGKDLAE MSLDELRKFS
KTIEQDVFEV LTLEGSVAAR NVHGGTAPAQ VRARIRAARA KLMPAKG
