ID R4VCQ3_9GAMM Unreviewed; 464 AA.
AC R4VCQ3;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=SPISAL_00150 {ECO:0000313|EMBL:AGM40131.1};
OS Spiribacter salinus M19-40.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Spiribacter.
OX NCBI_TaxID=1260251 {ECO:0000313|EMBL:AGM40131.1, ECO:0000313|Proteomes:UP000017881};
RN [1] {ECO:0000313|EMBL:AGM40131.1, ECO:0000313|Proteomes:UP000017881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M19-40 {ECO:0000313|EMBL:AGM40131.1};
RX PubMed=23409269;
RA Leon M.J., Ghai R., Fernandez A.B., Sanchez-Porro C., Rodriguez-Valera F.,
RA Ventosa A.;
RT "Draft Genome of Spiribacter salinus M19-40, an Abundant
RT Gammaproteobacterium in Aquatic Hypersaline Environments.";
RL Genome Announc. 1:E00179-12(2013).
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 -!- SIMILARITY: In the N-terminal section; belongs to the lyase 1 family.
CC Argininosuccinate lyase subfamily. {ECO:0000256|ARBA:ARBA00005552}.
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; CP005963; AGM40131.1; -; Genomic_DNA.
DR RefSeq; WP_016352438.1; NC_021291.1.
DR AlphaFoldDB; R4VCQ3; -.
DR KEGG; ssal:SPISAL_00150; -.
DR PATRIC; fig|1260251.3.peg.30; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_6; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000017881; 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:AGM40131.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017881}.
FT DOMAIN 12..306
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 369..436
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 464 AA; 50522 MW; F6EA3CD2BB5D7932 CRC64;
MSKADSKGMW GGRFSEATDD FVAAFTASEH YDRRLYRQDI RGSQAHARML ARCGVLSEAD
ATAIIDGLAA IAAEIEAGEF PWDPALEDVH MNIEARLTAR IGDAGKRLHT GRSRNDQIAT
DVRLWLREAI DEATHLLRHF QAGLVNLAER EADTVMPGFT HLQVAQPVSF GHHMLAWYEM
LVRDEARLAD ARVRVNQSPL GSAALAGTTF AIDREQTCAE LGFEAPTRNS LDAVSDRDFA
IEFVSAAALT MTHLSRMAEE LVLWASPLTG FIELPDRFCT GSSIMPQKKN PDVAELVRGK
SARVHGALNT LLTLMKGQPL AYNRDNQEDK EPLFDAADAL HDSLRAFGDM VPALSVNRER
TRQAARAGFA TATDLADYLV RKGVPFRDAH AIVGEAVAYG VQHGEDLSDL SLETLQGFSE
HIASDVYAVL TVDGSMAARD HLGGTAPAQV HQQVAAARAR LAGD
//