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Database: UniProt
Entry: A0A0D6DUP8_9LACT
LinkDB: A0A0D6DUP8_9LACT
Original site: A0A0D6DUP8_9LACT 
ID   A0A0D6DUP8_9LACT        Unreviewed;       462 AA.
AC   A0A0D6DUP8;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
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:CEN27508.1};
GN   ORFNames=LACPI_0308 {ECO:0000313|EMBL:CEN27508.1};
OS   Lactococcus piscium MKFS47.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=297352 {ECO:0000313|EMBL:CEN27508.1, ECO:0000313|Proteomes:UP000033166};
RN   [1] {ECO:0000313|Proteomes:UP000033166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MKFS47 {ECO:0000313|Proteomes:UP000033166};
RA   Andreevskaya M.;
RL   Submitted (JAN-2015) 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, 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}.
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DR   EMBL; LN774769; CEN27508.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D6DUP8; -.
DR   STRING; 1364.LP2241_10298; -.
DR   KEGG; lpk:LACPI_0308; -.
DR   HOGENOM; CLU_027272_2_3_9; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000033166; Chromosome I.
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}.
FT   DOMAIN          7..301
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          364..432
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   462 AA;  51572 MW;  EE4E6556467A85DD CRC64;
     MAKLWGGRFE AGLDKKTEAF GASITFDKKM ARQDLKGSLA HVTMLASTGI LTEQEAETIK
     AGIQKVEAKY EANEIDFKIE HEDIHMNMET YLHAEIGPVA GKLHTARSRN DQVATDMHLW
     VKDTLDETLD KLQNLREVLV DLASEHVETI MPGYTHLQHA QPISFGHHIM AYYSMLTRDA
     ERFTFNIKHA DISPLGAAAL AGTTFPIDRK ETAELMGFSD VYVNSIDAVS DRDFILEFLS
     NASLLMMHLS RLCEEIILWC SHEYKFVTLS DAFSTGSSIM PQKKNPDMAE LIRGKSGRVY
     GNLFGLLTVM KSLPLAYNKD LQEDKEGMFD TADTILTSLD VMSGMLSTMT VNEGIMSAST
     EKDFSNATEL ADYLAAKGLP FRQAHEIVGA MVLECTKAGN YLQDVPLSRY QEVSELIEAD
     IYDTLNSRTA VERRNSFGGT GFEQVKLQIE LARTTLQQDF KA
//
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