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Database: UniProt
Entry: A0A1C4VUY4_MICVI
LinkDB: A0A1C4VUY4_MICVI
Original site: A0A1C4VUY4_MICVI 
ID   A0A1C4VUY4_MICVI        Unreviewed;       485 AA.
AC   A0A1C4VUY4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338};
DE            EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338};
GN   ORFNames=GA0074695_1804 {ECO:0000313|EMBL:SCE87635.1};
OS   Micromonospora viridifaciens.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1881 {ECO:0000313|EMBL:SCE87635.1, ECO:0000313|Proteomes:UP000198242};
RN   [1] {ECO:0000313|EMBL:SCE87635.1, ECO:0000313|Proteomes:UP000198242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43909 {ECO:0000313|EMBL:SCE87635.1,
RC   ECO:0000313|Proteomes:UP000198242};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000985};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC       from L-ornithine and carbamoyl phosphate: step 3/3.
CC       {ECO:0000256|ARBA:ARBA00004941}.
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DR   EMBL; LT607411; SCE87635.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4VUY4; -.
DR   OrthoDB; 4899737at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000198242; Chromosome i.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR   Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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; ARGININOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR   Pfam; PF14698; ASL_C2; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; ARGSUCLYASE.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Lyase {ECO:0000313|EMBL:SCE87635.1}.
FT   DOMAIN          43..291
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          360..389
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   485 AA;  51209 MW;  5194824CB9357867 CRC64;
     MSTPALTTYQ RHHLAPTYDH HVGHLYPAMV RASQAHVVML TEQGLIPAER GARLLRGLAE
     LRADTGPAPA YDGSFEDTYY LMEKRLAEAC GIPTSELDVQ LARSRNDLDA GVFRMLLRDQ
     LLGVLDRVLA TGRTALDRAD RYADVVITGY THRRPAQPTT IGHALAGYAE ALAGEAAAYA
     DLIDQLNISP LGSCAFAGTD LDIAPARVAE LLGFAGLVTN SYEAVAGADH LVRVGTLNAQ
     ALATGARLAR TLMDWLSWNW VTTPADFTQG SSIMPQKRNP VVLEHLVSYA GAAAADAASV
     LNNVGAAWWE DSNNATTDVQ VRLWESNDRA ERFFALVGGF LAELAPLSPP SREEIVASGA
     TTTAAADALT RHGVPFRAAH SVVGRLVRAG APDTWTAEGV RAAAEGLTGP LDDAAVADLI
     AAAVRPDLVL NRAQVDGPGA AAVRAQVGTL RVAFDGVADR LAAVRDRLGR ADAALDAVAA
     ELVAR
//
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