ARLY_THET8
ID ARLY_THET8 Reviewed; 462 AA.
AC Q5SLL0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 109.
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=TTHA0283;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP008226; BAD70106.1; -; Genomic_DNA.
DR RefSeq; WP_011227830.1; NC_006461.1.
DR RefSeq; YP_143549.1; NC_006461.1.
DR PDB; 2E9F; X-ray; 2.80 A; A/B/C/D=1-462.
DR PDBsum; 2E9F; -.
DR AlphaFoldDB; Q5SLL0; -.
DR SMR; Q5SLL0; -.
DR STRING; 300852.55771665; -.
DR EnsemblBacteria; BAD70106; BAD70106; BAD70106.
DR GeneID; 3169422; -.
DR KEGG; ttj:TTHA0283; -.
DR PATRIC; fig|300852.9.peg.283; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_0; -.
DR OMA; KKNPDVF; -.
DR PhylomeDB; Q5SLL0; -.
DR UniPathway; UPA00068; UER00114.
DR EvolutionaryTrace; Q5SLL0; -.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW Lyase; Reference proteome.
FT CHAIN 1..462
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000240786"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 32..48
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 54..72
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:2E9F"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 110..146
FT /evidence="ECO:0007829|PDB:2E9F"
FT TURN 147..151
FT /evidence="ECO:0007829|PDB:2E9F"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:2E9F"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 168..193
FT /evidence="ECO:0007829|PDB:2E9F"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 212..218
FT /evidence="ECO:0007829|PDB:2E9F"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 228..233
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 236..262
FT /evidence="ECO:0007829|PDB:2E9F"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:2E9F"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 290..297
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 299..313
FT /evidence="ECO:0007829|PDB:2E9F"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 322..327
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 328..348
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 356..363
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 370..380
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 385..400
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 410..416
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 422..428
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:2E9F"
FT HELIX 445..459
FT /evidence="ECO:0007829|PDB:2E9F"
SQ SEQUENCE 462 AA; 51915 MW; C09724CFBB2DBA46 CRC64;
MAHRTWGGRF GEGPDALAAR FNASLAFDRA LWREDLWQNR VHARMLHAVG LLSAEELEAI
LKGLDRIEEE IEAGTFPWRE ELEDVHMNLE ARLTELVGPP GGKLHTARSR NDQVATDLRL
YLRGAIDELL ALLLALRRVL VREAEKHLDP LYVLPGYTHL QRAQPVLLAH WFLAYYEMLK
RDAGRLEDAK ERLNESPLGA AALAGTGFPI DRHFTARELG FKAPMRNSLD AVASRDFALE
VLSALNIGML HLSRMAEELI LYSTEEFGFV EVPDAFATGS SIMPQKKNPD ILELIRAKAG
RVLGAFVGLS AVVKGLPLAY NKDLQEDKEP LLDALATYRD SLRLLAALLP GLKWRRERMW
RAAEGGYTLA TELADYLAEK GLPFREAHHV VGRLVRRLVE EGRALKDLTL EELQAHHPLF
AEDALPLLRL ETAIHRRRSY GGTAPEAVRE RLEEAKKEVG LD
