GenomeNet

Database: UniProt
Entry: G6ECP1_9SPHN
LinkDB: G6ECP1_9SPHN
Original site: G6ECP1_9SPHN 
ID   G6ECP1_9SPHN            Unreviewed;       457 AA.
AC   G6ECP1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 59.
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=NSU_2112 {ECO:0000313|EMBL:EHJ60952.1};
OS   Novosphingobium pentaromativorans US6-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1088721 {ECO:0000313|EMBL:EHJ60952.1, ECO:0000313|Proteomes:UP000004030};
RN   [1] {ECO:0000313|EMBL:EHJ60952.1, ECO:0000313|Proteomes:UP000004030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=US6-1 {ECO:0000313|EMBL:EHJ60952.1,
RC   ECO:0000313|Proteomes:UP000004030};
RX   PubMed=22275104; DOI=10.1128/JB.06476-11;
RA   Luo Y.R., Kang S.G., Kim S.J., Kim M.R., Li N., Lee J.H., Kwon K.K.;
RT   "Genome sequence of benzo(a)pyrene-degrading bacterium Novosphingobium
RT   pentaromativorans US6-1.";
RL   J. Bacteriol. 194:907-907(2012).
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:EHJ60952.1}.
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; AGFM01000029; EHJ60952.1; -; Genomic_DNA.
DR   RefSeq; WP_007013027.1; NZ_CP009291.1.
DR   AlphaFoldDB; G6ECP1; -.
DR   STRING; 1088721.JI59_09525; -.
DR   KEGG; npn:JI59_09525; -.
DR   PATRIC; fig|1088721.3.peg.2091; -.
DR   eggNOG; COG0165; Bacteria.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000004030; 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|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|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00006};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004030}.
FT   DOMAIN          4..298
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          361..430
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   457 AA;  49397 MW;  2FC1446BCDFF96C3 CRC64;
     MWGGRFEGGP SAIMREINAS IPFDKALWRQ DIAASKAHVA MLGACGIVAG EDAVLISEGL
     DKVAAEYEAN GVPEDWDLED IHMTTESRLT ELIGPAAGRL HTARSRNDQV ATDFRLWVRD
     SIDQIDAGLE ALQVALVTRA GEHADSIMPG FTHLQTAQPV TLGHHLMAYY EMISRDRSRF
     ADARKRMNRS PLGSAALAGT GFPIDRKMTA QALGFDAPTD NSLDSVSDRD FALDYLMAAS
     QCSLHLSRLA EEFIIWASQP FGFVALPDAL STGSSIMPQK KNPDAAELVR GHAGRITGCL
     TALMMTMKGL PLAYSKDMQD DKPPVFEAAS LLALSVAAMT GMVADTRFRT DRMRGAAELG
     FATATDLADW LVREGNIPFR EAHHITGAAV KLAETRGLAL DQLPLSDLKE IDSRIDERVF
     KALSVEASVA ARNSHGGTAP DQVRLRVAEA RSALGLE
//
DBGET integrated database retrieval system