ARLY_GEOKA
ID ARLY_GEOKA Reviewed; 459 AA.
AC Q5KW95;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 25-MAY-2022, entry version 95.
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=GK2756;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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=BAD77041.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000043; BAD77041.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_021322121.1; NC_006510.1.
DR AlphaFoldDB; Q5KW95; -.
DR SMR; Q5KW95; -.
DR STRING; 235909.GK2756; -.
DR EnsemblBacteria; BAD77041; BAD77041; GK2756.
DR KEGG; gka:GK2756; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_9; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001172; 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..459
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137772"
SQ SEQUENCE 459 AA; 51553 MW; FBC5F940A4602228 CRC64;
MKKLWGGRFT KTAEEWVDEF GASIPFDQEL VEEDIEGSLA HVTMLGECGI LPEGDVEQIK
GGLIRLLEKA KQGELKFSIA YEDIHLNIEK MLIDDIGPVG GKLHTGRSRN DQVATDMHLY
LRKRVEEILG LIRGMQRALV AQAEKHVETI MPGYTHLQRA QPISFAHHLL AYFWMLERDY
ERFSESQKRI NRSPLGAGAL AGTTFPIDRH RTAELLGFAD IYENSLDAVS DRDFIIEFLS
NSSMLMMHLS RLAEELILWS SQEFQFIELD DAFATGSSIM PQKKNPDMAE LIRGKTGRVY
GHLMALLTVM KGLPLAYNKD MQEDKEGMFD TVKTVIGSLK IFTGMIETMN VRTDVMERAT
KQDFSNATEL ADYLAAKGVP FREAHEIVGK LVLHCIEQGV FLADLPLDVY KEASPLFEED
IYDALHPRTA VNRRNSAGGT GFAEVRAALA KAKQLLSTP
