ID A0A087B967_9BIFI Unreviewed; 501 AA.
AC A0A087B967;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=BMAGN_0767 {ECO:0000313|EMBL:KFI67567.1};
OS Bifidobacterium magnum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1692 {ECO:0000313|EMBL:KFI67567.1, ECO:0000313|Proteomes:UP000029052};
RN [1] {ECO:0000313|EMBL:KFI67567.1, ECO:0000313|Proteomes:UP000029052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11591 {ECO:0000313|EMBL:KFI67567.1,
RC ECO:0000313|Proteomes:UP000029052};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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:KFI67567.1}.
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DR EMBL; JGZB01000010; KFI67567.1; -; Genomic_DNA.
DR RefSeq; WP_022859353.1; NZ_JGZB01000010.1.
DR AlphaFoldDB; A0A087B967; -.
DR STRING; 1692.BMAGN_0767; -.
DR eggNOG; COG0165; Bacteria.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000029052; 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|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|HAMAP-Rule:MF_00006, ECO:0000313|EMBL:KFI67567.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029052}.
FT DOMAIN 22..317
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 380..452
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 501 AA; 54310 MW; D330C8C25EFB99FD CRC64;
MTDNTASQPS APQEEHLALW GGRFSSGPSA ALAKLSKSTQ FDWRLADDDI AGSRAHARAL
GRAGLLNGEE LNRMEQALDE LQRQVDSGEF EPREDDEDEA TALERGLLAI AGDELGGKLR
AGRSRNDQIA TLIRMWLRRH ARVIANLVLD TCDAIIDQAK RAGNTVMPGR THMQHAQPVL
LAHQLMAHVW PLLRDVQRLV DWDARINYSP YGAGALAGNT LGLSPMSVAQ ELGFANVTAN
SIDGTSSRDL VAEFSFVAAM IGVDLSRLSE EIIIWNSQEF SFVKLDDAYS TGSSIMPQKK
NPDIAELTRG KAGRLIGDLT GLLATLKGLP TAYARDLQED KEAVFDQVDT LEVVLPAFTG
MVATMVFQTE RLEQEAPTGF ALATDIAEWL VKNGVPFRHA HELSGACVKL AEGRGQELWD
LTDEDFVETF QEFVAPELAP EVRGVLSAAG SVSSRNGKGG TAPLRVREQI VAAKSETEAL
RAFGRSNSDG TAFKPAHSLK G
//
