ID A0A0D5VET2_9BURK Unreviewed; 468 AA.
AC A0A0D5VET2; A0A2T1AZD7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=BX589_10886 {ECO:0000313|EMBL:PRZ53956.1};
OS Paraburkholderia fungorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=134537 {ECO:0000313|EMBL:PRZ53956.1, ECO:0000313|Proteomes:UP000238376};
RN [1] {ECO:0000313|EMBL:PRZ53956.1, ECO:0000313|Proteomes:UP000238376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 28183 {ECO:0000313|EMBL:PRZ53956.1,
RC ECO:0000313|Proteomes:UP000238376};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) 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:PRZ53956.1}.
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DR EMBL; PVZM01000008; PRZ53956.1; -; Genomic_DNA.
DR RefSeq; WP_028196779.1; NZ_QFRC01000022.1.
DR STRING; 134537.OI25_666; -.
DR GeneID; 66514675; -.
DR KEGG; bfn:OI25_666; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000238376; 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|HAMAP-Rule:MF_00006, ECO:0000313|EMBL:PRZ53956.1}.
FT DOMAIN 15..308
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 371..443
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 468 AA; 51303 MW; 45DECF4E371E35D9 CRC64;
MTSQLHKKGE AWSARFSEPM SELVKRYTSS VFFDKRLALV DIEGSLAHAS MLAAQKIIAA
DDLAAIQRGM AQIKGEIERG EFEWQLDLED VHLNIEARLT ALIGDAGKRL HTGRSRNDQV
ATDIRLWLRG EIDRIGGLLT ELRTALLDMA EKNASTIMPG FTHLQVAQPV TFGHHLLAYV
EMFSRDAERM IDCRKRVNRL PLGAAALAGT SYPIDRHAVA KTLGFDGICA NSLDAVSDRD
FAIEFTAASA LVMTHVSRFS EELVLWMSPR VGFIDLADRF CTGSSIMPQK KNPDVPELAR
GKTGRVNGHL IALLTLMKGQ PLAYNKDNQE DKEPLFDTVD TVADTLRIFA EMVAGISVKP
QAMRDAALQG FSTATDLADY LVKRGLPFRD AHEAVALAVR VCADRGCDLA DLTLEEMRQE
LPNVAHLIGE DVFSYLTLEG SVASRNHPGG TAPEQVLAAV KAARAALK
//
