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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//