GenomeNet

Database: UniProt
Entry: G4R775_PELHB
LinkDB: G4R775_PELHB
Original site: G4R775_PELHB 
ID   G4R775_PELHB            Unreviewed;       500 AA.
AC   G4R775;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
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   OrderedLocusNames=KKY_182 {ECO:0000313|EMBL:AEQ50229.1};
OS   Pelagibacterium halotolerans (strain DSM 22347 / JCM 15775 / CGMCC 1.7692 /
OS   B2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Devosiaceae; Pelagibacterium.
OX   NCBI_TaxID=1082931 {ECO:0000313|EMBL:AEQ50229.1, ECO:0000313|Proteomes:UP000008850};
RN   [1] {ECO:0000313|EMBL:AEQ50229.1, ECO:0000313|Proteomes:UP000008850}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22347 / JCM 15775 / CGMCC 1.7692 / B2
RC   {ECO:0000313|Proteomes:UP000008850};
RX   PubMed=22156395; DOI=10.1128/JB.06343-11;
RA   Huo Y.Y., Cheng H., Han X.F., Jiang X.W., Sun C., Zhang X.Q., Zhu X.F.,
RA   Liu Y.F., Li P.F., Ni P.X., Wu M.;
RT   "Complete genome sequence of Pelagibacterium halotolerans B2T.";
RL   J. Bacteriol. 194:197-198(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   ---------------------------------------------------------------------------
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; CP003075; AEQ50229.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4R775; -.
DR   STRING; 1082931.KKY_182; -.
DR   KEGG; phl:KKY_182; -.
DR   PATRIC; fig|1082931.4.peg.182; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_5; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000008850; 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; 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.
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:UP000008850}.
FT   DOMAIN          46..303
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          368..406
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   500 AA;  55098 MW;  4026368C8FBB32DA CRC64;
     MASMRDTSVF PDPVYKETVL RPLFDGAKDH HADGFRAIDR AHLVMLAETG ILTRQQASSI
     ARALVAIDDE IDLDTLVYTG EVEDFFFLIE KNLKARLGPD LAGRLHTSRS RNDIDHTLFK
     LGLKPRTEML LEKMRVLLDA VLSTAEREAE TLIVAYTHGQ PAQPTTFGHY LGAMAEVLIR
     DIEKVESAIE VIDLSPMGAA AITTSGFPID RERVAELLGF ARPLENSYGC IASVDYITGI
     YGAMALSFLH LGRPIQDFQV WSSFEVGQLY VPNALVQISS IMPQKRNPVP IEHLRHLASQ
     TYGRAKAMLD IMHNTPFTDM NDSEGESQAM GYQVFDAAYR VLDLFTALIA QVSINPERVD
     INTKRSCITI TELADSLVRL EDLSFRQAHE VSAAVAKAVV AADGSLVEDG YAPFASAFEA
     ATGRASTLSP ERFAELVSAR HFVSVRDRLG GPAPTALRAS LGRYRQKLRG FFDQAARRTE
     TLKSAHKELN DKFNALLGAA
//
DBGET integrated database retrieval system