ID D4H6G2_DENA2 Unreviewed; 461 AA.
AC D4H6G2;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 01-MAY-2013, entry version 20.
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.
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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:HAMAP.
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; IPR003031; D_crystallin.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR000362; Fumarate_lyase.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR PANTHER; PTHR11444:SF3; PTHR11444:SF3; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-Aspartase-like; 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
//