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Database: UniProt
Entry: R4VCQ3_9GAMM
LinkDB: R4VCQ3_9GAMM
Original site: R4VCQ3_9GAMM 
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}.
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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
//
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