UniProt: D4JC85

Database: UniProt
Entry: D4JC85_9FIRM

LinkDB:  D4JC85_9FIRM 
Original site:  D4JC85_9FIRM

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (1)   
All databases (16)   

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ID   D4JC85_9FIRM            Unreviewed;       458 AA.
AC   D4JC85;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 65.
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=CC1_34310 {ECO:0000313|EMBL:CBK81956.1};
OS   Coprococcus catus GD/7.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Coprococcus.
OX   NCBI_TaxID=717962 {ECO:0000313|EMBL:CBK81956.1, ECO:0000313|Proteomes:UP000008798};
RN   [1] {ECO:0000313|EMBL:CBK81956.1, ECO:0000313|Proteomes:UP000008798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GD/7 {ECO:0000313|EMBL:CBK81956.1,
RC   ECO:0000313|Proteomes:UP000008798};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Coprococcus catus GD/7.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBK81956.1, ECO:0000313|Proteomes:UP000008798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GD/7 {ECO:0000313|EMBL:CBK81956.1,
RC   ECO:0000313|Proteomes:UP000008798};
RA   Pajon A.;
RL   Submitted (MAR-2010) 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}.
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DR   EMBL; FP929038; CBK81956.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4JC85; -.
DR   STRING; 717962.CC1_34310; -.
DR   KEGG; cct:CC1_34310; -.
DR   PATRIC; fig|717962.3.peg.3305; -.
DR   HOGENOM; CLU_027272_2_3_9; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000008798; 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|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|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00006}.
FT   DOMAIN          6..300
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          363..430
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   458 AA;  51697 MW;  1269A317D2F88CF1 CRC64;
     MKLWGGRFTK EENQLVHNFN ASITFDQKFY HQDIQGSIAH VTMLAKQAII TDAERDIIIS
     ALKEICSDIE SGKLQITEEY EDIHSFVESV LIERTGDTGK KLHTGRSRND QVALDMKLYT
     RDEVLATDEL VKELMTTLLD LMKEHIDTYM PGFTHLQKAQ PVTLAHHIGA YFEMFKRDRS
     RLHDIHERMN YCPLGAGALA GTTYPLDREY TASLLGFTGP TLNSMDSVSD RDYLIEYLSA
     LSTIMMHLSR FCEEIILWNS NEYRFIELDD AYSTGSSIMP QKKNPDIAEL IRGKTGRVYG
     ALTSLLTTMK GLPLAYNKDM QEDKELTFDA IDTVKGCLAL FNGMIKTMHV NKETMAASSK
     NGFTNATDAA DYLVKHGVPF RDAHGIIGQL VLICIDKGIA LDDLPLEEYK KISPVFEEDV
     YEAISMKTCV SLRQTIGAPG HEAMQKVIDI NSRYLEEN
//

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