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Database: UniProt
Entry: G8UKY2_TANFA
LinkDB: G8UKY2_TANFA
Original site: G8UKY2_TANFA 
ID   G8UKY2_TANFA            Unreviewed;       445 AA.
AC   G8UKY2;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
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:AEW21258.1};
GN   OrderedLocusNames=BFO_0473 {ECO:0000313|EMBL:AEW21258.1};
OS   Tannerella forsythia (strain ATCC 43037 / JCM 10827 / CCUG 21028 A / KCTC
OS   5666 / FDC 338) (Bacteroides forsythus).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Tannerella.
OX   NCBI_TaxID=203275 {ECO:0000313|EMBL:AEW21258.1, ECO:0000313|Proteomes:UP000005436};
RN   [1] {ECO:0000313|Proteomes:UP000005436}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43037 / JCM 10827 / CCUG 33226 / KCTC 5666 / FDC 338
RC   {ECO:0000313|Proteomes:UP000005436};
RA   Dewhirst F., Tanner A., Izard J., Brinkac L., Durkin A.S., Hostetler J.,
RA   Shetty J., Torralba M., Gill S., Nelson K.;
RT   "Complete sequence of Tannerella forsythia ATCC 43037.";
RL   Submitted (DEC-2011) 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; CP003191; AEW21258.1; -; Genomic_DNA.
DR   RefSeq; WP_014223929.1; NC_016610.1.
DR   AlphaFoldDB; G8UKY2; -.
DR   STRING; 203275.BFO_0473; -.
DR   GeneID; 34757849; -.
DR   KEGG; tfo:BFO_0473; -.
DR   PATRIC; fig|203275.8.peg.423; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_0_10; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000005436; 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; 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; 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|HAMAP-Rule:MF_00006, ECO:0000313|EMBL:AEW21258.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005436}.
FT   DOMAIN          28..303
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
SQ   SEQUENCE   445 AA;  50542 MW;  AE31A2DAA1C98D77 CRC64;
     MSRKLWEKNI QVDKEVERFT VGKDRELDLY LAPYDMLGSM AHITMLESIG LLTKDELQSL
     HAELKNMYAE AEHGNFVIEE GVEDVHSQVE LMLTRKLGDI GKKIHSGRSR NDQVLLDLKL
     FTRARIRELV RLTRDLFEVL IDQSNRYKDI LMPGYTHLQI AMPSSFGLWF AAYAESLADD
     LLLMQAAYKI CNRNPLGSAA GYGSSFPLNR SMTTELLGFD SMNYNVVYAQ MGRGKMERTV
     AYAMAGIAAT LSKLAMDACL FNSQNFGFIQ LPDSFTTGSS IMPHKKNPDV FELTRAKCNT
     LQGMPQQIAL ICNNLPSGYF RDLQIIKELF LPSFDELNDC LRMVTLMMRE IKINEHILDD
     PKYSLLFSVE EVNRLVMDGV PFRDAYKKVG MDIEAGTFTA DQTVRHTHEG SMGNLCNEKI
     EQLMQQTIEG FQFEKVDRAE KGLLA
//
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