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Database: UniProt
Entry: A0A165YJ25_9BACI
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ID   A0A165YJ25_9BACI        Unreviewed;       456 AA.
AC   A0A165YJ25;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=AP3564_19445 {ECO:0000313|EMBL:ASS92152.1}, AZI98_06125
GN   {ECO:0000313|EMBL:KZN97131.1};
OS   Aeribacillus pallidus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Aeribacillus.
OX   NCBI_TaxID=33936 {ECO:0000313|EMBL:KZN97131.1, ECO:0000313|Proteomes:UP000076476};
RN   [1] {ECO:0000313|EMBL:KZN97131.1, ECO:0000313|Proteomes:UP000076476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8m3 {ECO:0000313|EMBL:KZN97131.1,
RC   ECO:0000313|Proteomes:UP000076476};
RA   Poltaraus A.B., Nazina T.N., Tourova T.P., Malakho S.M., Korshunova A.V.,
RA   Sokolova D.S.;
RT   "Draft genome sequence of Aeribacillus pallidus 8m3 from petroleum
RT   reservoir.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ASS92152.1, ECO:0000313|Proteomes:UP000214606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC3564 {ECO:0000313|EMBL:ASS92152.1,
RC   ECO:0000313|Proteomes:UP000214606};
RA   Lee Y.-J., Park M.-K., Yi H., Bahn Y.-S., Kim J.F., Lee D.-W.;
RT   "The whole genome sequencing and assembly of Aeribacillus pallidus KCTC3564
RT   strain.";
RL   Submitted (OCT-2016) 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; CP017703; ASS92152.1; -; Genomic_DNA.
DR   EMBL; LWBR01000013; KZN97131.1; -; Genomic_DNA.
DR   RefSeq; WP_063387385.1; NZ_LWBR01000013.1.
DR   STRING; 33936.AZI98_06125; -.
DR   KEGG; apak:AP3564_19445; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000076476; Unassembled WGS sequence.
DR   Proteomes; UP000214606; 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|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   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:UP000076476}.
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   456 AA;  51777 MW;  265934FE5D89317B CRC64;
     MKKLWGGRFQ KTPEAWVDEF NASITFDKQL VEEDIQGSLA HVKMLAKCGI LTKEEGEAIE
     KGLHRLLEKA KNGELEYSVQ YEDIHLNIEK MLIDEIGPIG GKLHTSRSRN DQVATDMHLY
     LKKHVEAIVE LIRELQKALV NKAEQHIETI LPGYTHLQRA QPVSFAHHLL AYFWMLERDK
     SRFTESLKRI NISPLGAAAL AGTTFPIDRK YTAELLGFDE VYLNSLDAVS DRDFIVEFMS
     NSSLLMIHLS RFCEELILWC SQEFQFVEMD DAYSTGSSIM PQKKNPDMAE LIRGKSGRVV
     GNLVGLLTVL KGLPLAYNKD LQEDKEGMFD TVKTVEGCLQ IMTGMIETLK VNKEQMEKSV
     KQDFSNATEL ADYLAKKGLP FREAHEVVGK LVYKCIQKGI YLLDLPLEEY KEASSLFEND
     VYEVLNPYEA VNKRNSLGGT GFKEVKEQIN KAKAII
//
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