ARLY_GEOTN
ID ARLY_GEOTN Reviewed; 459 AA.
AC A4IRS2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 86.
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=GTNG_2681;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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; CP000557; ABO68026.1; -; Genomic_DNA.
DR RefSeq; WP_011887968.1; NC_009328.1.
DR AlphaFoldDB; A4IRS2; -.
DR SMR; A4IRS2; -.
DR STRING; 420246.GTNG_2681; -.
DR EnsemblBacteria; ABO68026; ABO68026; GTNG_2681.
DR KEGG; gtn:GTNG_2681; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_9; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 751464at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001578; 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.
FT CHAIN 1..459
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000000481"
SQ SEQUENCE 459 AA; 51608 MW; EB79623E9C3068F1 CRC64;
MKKLWGGRFT KTAEEWVDEF GASIPFDQEL VEEDIEGSLA HVTMLGECGI LPAEDVEKIK
DGLLRLLEKA KRGELEFSVA YEDIHLNIEK MLIDDIGSVG GKLHTGRSRN DQVATDMHLY
LRKRVKEILS LIRGLQRALV SQAEKHVETI MPGYTHLQRA QPISFAHHLL AYVWMLERDY
ERFSESLKRI NRSPLGAGAL AGTTFPINRQ RTAELLGFEG IYENSLDAVS DRDFIIEFLS
NSSMLMMHLS RLAEELILWS SQEFQFVELD DAFATGSSIM PQKKNPDMAE LIRGKTGRVY
GHLMALLTVM KGLPLAYNKD MQEDKEGMFD TVKTVIGSLK IFTGMIETMN VRVDAMEKAT
KQDFSNATEL ADYLAAKGMP FREAHEVVGK LVLHCIEQGV FLADLPLEVY KEASPLFEKD
IYDALNPRTA VNRRNSAGGT GFAEVRATLA KVKERLGTL
