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Database: UniProt
Entry: A0A0D6MHU2_9PROT
LinkDB: A0A0D6MHU2_9PROT
Original site: A0A0D6MHU2_9PROT 
ID   A0A0D6MHU2_9PROT        Unreviewed;       445 AA.
AC   A0A0D6MHU2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
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=Tasa_009_014 {ECO:0000313|EMBL:GAN53219.1};
OS   Tanticharoenia sakaeratensis NBRC 103193.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Tanticharoenia.
OX   NCBI_TaxID=1231623 {ECO:0000313|EMBL:GAN53219.1, ECO:0000313|Proteomes:UP000032679};
RN   [1] {ECO:0000313|EMBL:GAN53219.1, ECO:0000313|Proteomes:UP000032679}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 103193 {ECO:0000313|EMBL:GAN53219.1,
RC   ECO:0000313|Proteomes:UP000032679};
RA   Azuma Y., Hadano H., Hirakawa H., Matsushita K.;
RT   "Genome sequencing of Tanticharoenia sakaeratensis NBRC 103193.";
RL   Submitted (OCT-2012) 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}.
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:GAN53219.1}.
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DR   EMBL; BALE01000009; GAN53219.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D6MHU2; -.
DR   STRING; 1231623.Tasa_009_014; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000032679; 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:UP000032679}.
FT   DOMAIN          1..285
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          348..416
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   445 AA;  48125 MW;  717B39AD6663FB7A CRC64;
     MAEINASIGF DRALWRQDIR GSLAHARMLS AQGIITPDDE AAIRAGLADI AGEIEAGRFD
     FDPGLEDIHM NIEARLSERI GEPGKRLHTA RSRNDQVATD FRLWVRDAID AIDARLVSLM
     RALSTRAMEF HATPMPGFTH LQVAQPVTFG HHLLAYVEML ARDRGRLSDA RARLNECPLG
     SAALAGTSFP IDRHATAQAL GFDRPTANSL DSVSDRDFAL EYLSALSILG IHLSRFAEEI
     VIWCSGPYGF VTLSDAFTTG SSIMPQKRNP DAAELVRAKI GRIAGHLIGL MTVMKGLPLA
     YAKDMQEDKE PVFAATDAAM LSIAATDGMV RDLAPNVERL RLFAGSGFAT ATDLADWLVR
     VLKMPFRNAH HVTGKLVAMA EARGCDLSGL SLADMQSVEP AITDDVFSVL TVEASLASRT
     SHGGTAPSNV ARAAQLWIDR LGEDA
//
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