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Database: UniProt
Entry: L0MMP2_9GAMM
LinkDB: L0MMP2_9GAMM
Original site: L0MMP2_9GAMM 
ID   L0MMP2_9GAMM            Unreviewed;       457 AA.
AC   L0MMP2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 61.
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=D781_4443 {ECO:0000313|EMBL:AGB84607.1};
OS   Serratia sp. FGI94.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=671990 {ECO:0000313|EMBL:AGB84607.1, ECO:0000313|Proteomes:UP000011001};
RN   [1] {ECO:0000313|EMBL:AGB84607.1, ECO:0000313|Proteomes:UP000011001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGI94 {ECO:0000313|EMBL:AGB84607.1,
RC   ECO:0000313|Proteomes:UP000011001};
RX   PubMed=23516234;
RA   Aylward F.O., Tremmel D.M., Starrett G.J., Bruce D.C., Chain P., Chen A.,
RA   Davenport K.W., Detter C., Han C.S., Han J., Huntemann M., Ivanova N.N.,
RA   Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M., Pagani I., Pati A.,
RA   Pitluck S., Teshima H., Deshpande S., Goodwin L., Woyke T., Currie C.R.;
RT   "Complete Genome of Serratia sp. Strain FGI 94, a Strain Associated with
RT   Leaf-Cutter Ant Fungus Gardens.";
RL   Genome Announc. 1:E0023912-E0023912(2013).
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   -!- SIMILARITY: In the N-terminal section; belongs to the lyase 1 family.
CC       Argininosuccinate lyase subfamily. {ECO:0000256|ARBA:ARBA00005552}.
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DR   EMBL; CP003942; AGB84607.1; -; Genomic_DNA.
DR   RefSeq; WP_015962303.1; NC_020064.1.
DR   AlphaFoldDB; L0MMP2; -.
DR   KEGG; smaf:D781_4443; -.
DR   PATRIC; fig|1249634.3.peg.4256; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_6; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000011001; 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|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:AGB84607.1}.
FT   DOMAIN          6..301
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          364..431
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   457 AA;  50100 MW;  64B7DFB9D5613CB9 CRC64;
     MALWGGRFSQ AADQRFKHLN DSLRFDYRLA EQDIVGSVAW SKALATVNVL TVQEQQQLEQ
     ALNALLTEVQ ADPLAIVQSD AEDIHSWVEQ KLIEKVGDLG KKLHTGRSRN DQVATDLKLW
     CKQQVGDLLT AIVQLQQALV ETAEANQDAV MPGYTHLQRA QPVTFAHWCL AYVEMLARDE
     SRLQDTLQRL DVSPLGCGAL AGTAYPIDRE QLAGWLGFAS ATRNSLDSVS DRDHVLELLS
     NASISMVHLS RFAEDLIFFN SGEADFIELS DRVTSGSSLM PQKKNPDALE LIRGKCGRVQ
     GALTGMMMTL KGLPLAYNKD MQEDKEGLFD ALDTWMDCLQ MAALVLDGIQ VKRPRCQEAA
     EQGYANATEL ADYLVAKGVP FREAHHIVGE AVVEAIRQGK ALEALPLADL QQFSSVIGDD
     VYPVLSLQSC LDKRSAKGGV SPQQVASAIA AAKQRLA
//
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