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ARLY_DESVM
ID   ARLY_DESVM              Reviewed;         460 AA.
AC   B8DN65;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=DvMF_0048;
OS   Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=883;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19637 / Miyazaki F;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA   Richardson P.;
RT   "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL   Submitted (OCT-2008) 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}.
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DR   EMBL; CP001197; ACL07009.1; -; Genomic_DNA.
DR   RefSeq; WP_012611217.1; NC_011769.1.
DR   AlphaFoldDB; B8DN65; -.
DR   SMR; B8DN65; -.
DR   STRING; 883.DvMF_0048; -.
DR   EnsemblBacteria; ACL07009; ACL07009; DvMF_0048.
DR   KEGG; dvm:DvMF_0048; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_7; -.
DR   OMA; KKNPDVF; -.
DR   OrthoDB; 751464at2; -.
DR   UniPathway; UPA00068; UER00114.
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..460
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000116203"
SQ   SEQUENCE   460 AA;  50486 MW;  4F7183B0BE5D2E36 CRC64;
     MAEKKMWGGR FRQATAALVE EYTQSVSFDR ALYAQDIAGS KAHARMLAKQ GVLTADEAAR
     IVEGLDMVLA EIEGGTFVWR RELEDVHMNI ESRLTELVGD VGKKLHTGRS RNDQVALDFR
     LFVSDRIRAW RGLARDLVAV LAERAGEHAN TLLPGCTHMQ PAQPVSLGHH LLAYAWMLRR
     DAERLADCDR RTRVCPLGAA ALAGTTYPLD PAYVAEQLDM YGTFRNSMDA VSDRDFVLES
     LFCGATIMAH LSRLCEEIII WANPAFGFVR LPDAYATGSS IMPQKKNPDV AEIMRGKTGR
     VYGALTAMLT TVKGLPMTYN RDMQEDKEPF LDCDRTVSAS LEIMAGMLRE LGFNEGRMRA
     ALRAGFLNAT ELADYLVGKG IPFREAHHLT GAAVALAEER AITLEELPLA DLQAICDRIG
     DDVYAVLDPA AAVARREMPG GTGPASVAAQ LAELSGWLEE
 
 
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