GenomeNet

Database: UniProt/TrEMBL
Entry: D4H6G2_DENA2
LinkDB: D4H6G2_DENA2
Original site: D4H6G2_DENA2 
ID   D4H6G2_DENA2            Unreviewed;       461 AA.
AC   D4H6G2;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   19-FEB-2014, entry version 22.
DE   RecName: Full=Argininosuccinate lyase;
DE            Short=ASAL;
DE            EC=4.3.2.1;
DE   AltName: Full=Arginosuccinase;
DE   Flags: Precursor;
GN   Name=argH; OrderedLocusNames=Dacet_2886;
OS   Denitrovibrio acetiphilus (strain DSM 12809 / N2460).
OC   Bacteria; Deferribacteres; Deferribacterales; Deferribacteraceae;
OC   Denitrovibrio.
OX   NCBI_TaxID=522772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12809 / N2460;
RX   DOI=10.4056/sigs.892105;
RA   Kiss H., Lang E., Lapidus A., Copeland A., Nolan M.,
RA   Glavina Del Rio T., Chen F., Lucas S., Tice H., Cheng J., Han C.,
RA   Goodwin L., Pitluck S., Liolios K., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.,
RA   Jeffries C., Detter J., Brettin T., Spring S., Rohde M., Goker M.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H.;
RT   "Complete genome sequence of Denitrovibrio acetiphilus type strain
RT   (N2460).";
RL   Stand. Genomic Sci. 2:270-279(2010).
CC   -!- CATALYTIC ACTIVITY: 2-(N(omega)-L-arginino)succinate = fumarate +
CC       L-arginine.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       arginine from L-ornithine and carbamoyl phosphate: step 3/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001968; ADD69636.1; -; Genomic_DNA.
DR   RefSeq; YP_003505592.1; NC_013943.1.
DR   ProteinModelPortal; D4H6G2; -.
DR   EnsemblBacteria; ADD69636; ADD69636; Dacet_2886.
DR   GeneID; 8877268; -.
DR   KEGG; dap:Dacet_2886; -.
DR   PATRIC; 35355805; VBIDenAce54242_2889.
DR   HOGENOM; HOG000242744; -.
DR   KO; K01755; -.
DR   BioCyc; DACE522772:GHC2-2933-MONOMER; -.
DR   UniPathway; UPA00068; UER00114.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR   Gene3D; 1.10.275.10; -; 1.
DR   HAMAP; MF_00006; Arg_succ_lyase; 1.
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   PANTHER; PTHR11444; PTHR11444; 1.
DR   PANTHER; PTHR11444:SF3; PTHR11444:SF3; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR00838; argH; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome;
KW   Cytoplasm; Lyase.
SQ   SEQUENCE   461 AA;  52084 MW;  8466C793E7DB4503 CRC64;
     MSEKMWGGRF SLPTDKFVEE FNASVHFDNR FYKYDIKGSI AHAKMLAKQE IISTEDRDSI
     IKGLNQVLQE IETGKLEWKT EDEDIHMAVE KRLTELVGDA GKRLHTARSR NDQVAVDFRM
     YLKAEIIEIQ ALIAELLNTL MKKAEAEHEV MMPGFTHLQT AQPILFAHWA MAYFQMIKRD
     FSRFADCLER MDFCPLGAGA LAGTTFNIDR HFTAAELGFK APTENSLDSV SDRDFALEFL
     AACSICQMHL SRFSEELIIY SASEFSFIEL SDDFCTGSSI MPQKKNPDMP ELIRGKTGRV
     YGSLISLLTT MKGLPLAYNK DMQEDKEPVF DAVDTIKASL KIFSPMVEKM TLRKDKMEKS
     AGNGYSTATD LADYLVRKGV PFRQSHHIVG SAVAYAIEKG VDLSELSMDE FARFTDVITD
     DIYQYITVRA SVNSRVAYGG TAESSVKEQI KSAKKFLNEI Y
//
DBGET integrated database retrieval system