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Database: UniProt
Entry: V6JU13_STRNV
LinkDB: V6JU13_STRNV
Original site: V6JU13_STRNV 
ID   V6JU13_STRNV            Unreviewed;       475 AA.
AC   V6JU13;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE            Short=ASAL {ECO:0000256|HAMAP-Rule:MF_00006};
DE            EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE   AltName: Full=Arginosuccinase {ECO:0000256|HAMAP-Rule:MF_00006};
GN   Name=argH {ECO:0000256|HAMAP-Rule:MF_00006};
GN   ORFNames=M877_34220 {ECO:0000313|EMBL:EST20379.1};
OS   Streptomyces niveus NCIMB 11891.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1352941 {ECO:0000313|EMBL:EST20379.1, ECO:0000313|Proteomes:UP000017971};
RN   [1] {ECO:0000313|EMBL:EST20379.1, ECO:0000313|Proteomes:UP000017971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 11891 {ECO:0000313|EMBL:EST20379.1,
RC   ECO:0000313|Proteomes:UP000017971};
RX   PubMed=24407644;
RA   Flinspach K., Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT   "Draft Genome Sequence of Streptomyces niveus NCIMB 11891, Producer of the
RT   Aminocoumarin Antibiotic Novobiocin.";
RL   Genome Announc. 2:e01146-e01113(2014).
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, ECO:0000256|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.
CC       {ECO:0000256|ARBA:ARBA00004941, ECO:0000256|HAMAP-Rule:MF_00006}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00006}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EST20379.1}.
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DR   EMBL; AWQW01000267; EST20379.1; -; Genomic_DNA.
DR   RefSeq; WP_023542897.1; NZ_CM002280.1.
DR   AlphaFoldDB; V6JU13; -.
DR   STRING; 193462.BBN63_28875; -.
DR   PATRIC; fig|1352941.4.peg.6943; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_2_11; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000017971; 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; 1.10.40.30; 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   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   NCBIfam; TIGR00838; argH; 1.
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   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00006};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW   Rule:MF_00006}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000313|EMBL:EST20379.1}.
FT   DOMAIN          20..309
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          372..439
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   475 AA;  50824 MW;  A2EB0E15E4A55B6D CRC64;
     MSSNTGDVRL WGGRFADGPA EALAKLSASV HFDWRLAPYD IAGSRAHARV LNKAGLLTED
     ELDRMIAGLD RLEAAVADGS FTGTVADEDV HTALERGLLE QLGADLGGKL RAGRSRNDQV
     ATLFKMYLRD HARIIGALIA DLQDALVGLA EAHPDVAMPG RTHLQHAQPV LFAHHVLAHV
     QSLSRDAERL RQWDERTAVS PYGSGALAGS SLGLDPEAVA ADLGFERGSA ANSIDGTAAR
     DFAAEFAFIT AMIGVNLSRI AEEVIIWNTK EFSFVTLHDA FSTGSSIMPQ KKNPDIAELA
     RGKSGRLIGN LTGLLATLKA LPLAYNRDLQ EDKEPVFDSC DQLEVLLPAF TGMMATLTVN
     RERMAELAPA GFSLATDIAE WLVRQGVPFR VAHEVAGECV KVCEKEGIEL DELTDDQFAS
     ISGHLTPEVR TVLDVSGALA SRDGRGGTAP SAVAVQLAEV KTDLAIQHAW ATAKK
//
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