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Database: UniProt
Entry: A0A0N0CSL9_9LACO
LinkDB: A0A0N0CSL9_9LACO
Original site: A0A0N0CSL9_9LACO 
ID   A0A0N0CSL9_9LACO        Unreviewed;       465 AA.
AC   A0A0N0CSL9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
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   ECO:0000313|EMBL:KOY76015.1};
GN   ORFNames=RZ71_04490 {ECO:0000313|EMBL:KOY76015.1};
OS   Apilactobacillus kunkeei.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Apilactobacillus.
OX   NCBI_TaxID=148814 {ECO:0000313|EMBL:KOY76015.1, ECO:0000313|Proteomes:UP000037778};
RN   [1] {ECO:0000313|EMBL:KOY76015.1, ECO:0000313|Proteomes:UP000037778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LAko {ECO:0000313|EMBL:KOY76015.1,
RC   ECO:0000313|Proteomes:UP000037778};
RX   PubMed=25953738; DOI=10.1093/gbe/evv079;
RA   Tamarit D., Ellegaard K.M., Wikander J., Olofsson T., Vasquez A.,
RA   Andersson S.G.;
RT   "Functionally Structured Genomes in Lactobacillus kunkeei Colonizing the
RT   Honey Crop and Food Products of Honeybees and Stingless Bees.";
RL   Genome Biol. Evol. 7:1455-1473(2015).
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:KOY76015.1}.
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DR   EMBL; JXCY01000007; KOY76015.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0CSL9; -.
DR   PATRIC; fig|148814.8.peg.1375; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000037778; Unassembled WGS sequence.
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|HAMAP-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|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00006};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037778}.
FT   DOMAIN          8..302
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          365..432
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   465 AA;  52816 MW;  FC1E11F8E64BA84B CRC64;
     MSEKLWGGRF NGDANDLFLR LGASINVDIK MANEDIEGSI AHATMLSHVG IITEAEKDQI
     VNGLKEIKEE FNEGKLHFTY QNEDIHMNVE TVLTEKIGAV AGKLHTARSR NDQVALDFHL
     YLKKRLPQIL ELIRSFQSEL VNLADENLET IMPGYTHLQH AQPISFAHYL MAYYEMLDRD
     YDRFEFNQKH TNMSPIGAAA LAGTTFPIDP HFTANELGLD APYNNSIDAV SDRDFAIEFL
     SNASILMMHL SRLCEEICLW SSYEFKYVEL SDAFSTGSSI MPQKKNPDMC ELIRGKTGVV
     YGHLNALLAT MKSLPLAYNK DLQEDKAGVF DTVENIEPIL QLMTEMIATM QVNKDRMLQA
     VEKDFSNATE LADYLSAKGL PFRQAHRIAG ELVAKCINEN CYLQDLSLEQ LHNYSDLFEE
     DIYEDLKPHV AIQRRKSYGS TGFNEVHKQI EKAKEKLKGE MNHEE
//
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