ARLY_SYNAS
ID ARLY_SYNAS Reviewed; 472 AA.
AC Q2LT96;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 94.
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=SYNAS_14300;
GN ORFNames=SYN_02158;
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB;
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(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; CP000252; ABC77309.1; -; Genomic_DNA.
DR RefSeq; WP_011417331.1; NC_007759.1.
DR AlphaFoldDB; Q2LT96; -.
DR SMR; Q2LT96; -.
DR STRING; 56780.SYN_02158; -.
DR PRIDE; Q2LT96; -.
DR EnsemblBacteria; ABC77309; ABC77309; SYN_02158.
DR KEGG; sat:SYN_02158; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_7; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 751464at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001933; 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..472
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000240784"
SQ SEQUENCE 472 AA; 53888 MW; 5F406867D917A6F4 CRC64;
MKDSTEKSKP WGGRFQEPTN ELVEAFTASI SFDRRLYRYD IEGSIAHARM LVRQEIINRK
EGFAIVEGLK EIQRDIETGS FEFSPGDEDI HMAIEKDLIR RIGDAGAKLH TGRSRNDQVA
LDVRLYLRAE IKEILEFMKV LKGAFLELAK KEAETILPGY THLQKAQPVL LAHYLLAWRE
MLDRDESRLR DCYRRVNVLP LGAAALAGTS LPIDRAYVAR LLKFPEISRN SMDTVSDRDF
VAEFLFASSL IMMHLSRFCE DLILWSSGEF NFVEISDAFT TGSSIMPQKK NPDVAELIRG
KTGRVYGNLI ALLTLLKGLP MTYNRDLQED KEPLFDTVDT VKACLQILAE MIRNMKFNRE
KMRQEAEGGF STATDLAEYL VMKGIPFREA HGIVGKLVSF CIECKKELAQ LSMEEFQRFC
PVINEDIHDR LSVSNSVRSR KSYGGTACRQ VMEQIRQIEE GAYPSTRRRK EA
