ID F7T998_9BURK Unreviewed; 507 AA.
AC F7T998;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=AXXA_27720 {ECO:0000313|EMBL:EGP43058.1};
OS Achromobacter insuavis AXX-A.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=1003200 {ECO:0000313|EMBL:EGP43058.1, ECO:0000313|Proteomes:UP000004853};
RN [1] {ECO:0000313|EMBL:EGP43058.1, ECO:0000313|Proteomes:UP000004853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AXX-A {ECO:0000313|EMBL:EGP43058.1,
RC ECO:0000313|Proteomes:UP000004853};
RA Bador J., Amoureux L., Neuwirth C.;
RL Submitted (JUN-2011) 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:EGP43058.1}.
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DR EMBL; AFRQ01000133; EGP43058.1; -; Genomic_DNA.
DR RefSeq; WP_006395527.1; NZ_GL982453.1.
DR AlphaFoldDB; F7T998; -.
DR PATRIC; fig|1003200.3.peg.5484; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_4; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000004853; 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; 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.
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:EGP43058.1}.
FT DOMAIN 54..304
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 368..445
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 507 AA; 55023 MW; 8807F6D6CBEC7893 CRC64;
MESKVSARLK QPLAKEVLEH LFLPRLNREF FANFDMLTQI NLAHLLMLRE RGILDHDAAR
RLAQALLQMQ ADGPHAVELD PAREEAYFNY EAHLIKAVGQ ELGGRLHTAR SRNDIGATID
RMRARDFTAR IGSALIGVSR AALAQAERYA DCVMPGYTHM QAAQPITYGY YLSALVDAWS
RDIGRLAHVL ETADASPLGA CALAGTSFPI DRDSTSAMLG FSGPLANALD SVASRDFALE
LSATLSIMMV TCSRMVQDFY IWSTPEFGYL SFPDSIASTS SIMPQKKNPA VLEYLRGKTG
HLIGLTSAAL STVKSTHFTH SGDSSRESTR TCWEGCEEAL KALELVQLLV EQVAPNRERM
VARAADDFST VTDLADLLVR KADASFRDAH HIIGAVVRQA LEQGLPARAI APAMIAAAAQ
EQLGRPVALA ADDIAACLDP ERNVAARLSL GGPAPQSVRA HLREQHAILD ARQAAIDAAR
QRAADARETL QGRVNALVHQ ENGMATA
//
