ID A0A1W6SKG6_9PROT Unreviewed; 470 AA.
AC A0A1W6SKG6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=EBAPG3_000015 {ECO:0000313|EMBL:ARO86297.1};
OS Nitrosospira lacus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=1288494 {ECO:0000313|EMBL:ARO86297.1, ECO:0000313|Proteomes:UP000012179};
RN [1] {ECO:0000313|EMBL:ARO86297.1, ECO:0000313|Proteomes:UP000012179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APG3 {ECO:0000313|EMBL:ARO86297.1,
RC ECO:0000313|Proteomes:UP000012179};
RX PubMed=25336720; DOI=10.1099/ijs.0.070789-0;
RA Urakawa H., Garcia J.C., Nielsen J.L., Le V.Q., Kozlowski J.A., Stein L.Y.,
RA Lim C.K., Pommerening-Roser A., Martens-Habbena W., Stahl D.A., Klotz M.G.;
RT "Nitrosospira lacus sp. nov., a psychrotolerant, ammonia-oxidizing
RT bacterium from sandy lake sediment.";
RL Int. J. Syst. Evol. Microbiol. 65:242-250(2015).
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 ---------------------------------------------------------------------------
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; CP021106; ARO86297.1; -; Genomic_DNA.
DR RefSeq; WP_004180343.1; NZ_CP021106.3.
DR AlphaFoldDB; A0A1W6SKG6; -.
DR KEGG; nlc:EBAPG3_000015; -.
DR eggNOG; COG0165; Bacteria.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000012179; 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:ARO86297.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000012179}.
FT DOMAIN 20..314
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 377..445
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 470 AA; 51994 MW; 0747FB5DAD7CF3B7 CRC64;
MATSKKKSTS AEKKGNTWSG RFDEPVSELV QRYTASVGFD RRLAEYDIQG SLAHARMLSG
AGIIDAGDLA AIESGLGLIR DEIRSGEFVW LLELEDVHLN IEKRLTTLIG DAGKRLHTAR
SRNDQVATDV RLYLRAAIDD IIGLIQGMQR ALLDLAERHV DTVMPGFTHL QVAQPVVFGH
HLMAYFEMLK RDVERLSDCR RRVNKLPLGA AALAGTSYPI NRKAVAQQLG FDGVCENSLD
AVSDRDFAIE FCAGAALIMT HLSRLSEELI LWMNPSFGFI DLADRFCTGS SIMPQKKNPD
VPELVRGKTG RVNGHLVALL TLMKGQPLAY NKDNQEDKEP LFDTVETLID TLRIYADMLT
GVRVNQEVMR NAAMRGYATA TDLADYLTKK GLPFREAHEA VAQAVRFADK SGRDLSALSL
PELQKFSRLI DSDIYAVLTL EGSINSRSHI GGTAPAQVRA AIRRARKWLS
//
