ID ARLY_ACAM1 Reviewed; 476 AA.
AC B0CEZ5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 01-MAY-2013, entry version 41.
DE RecName: Full=Argininosuccinate lyase;
DE Short=ASAL;
DE EC=4.3.2.1;
DE AltName: Full=Arginosuccinase;
GN Name=argH; OrderedLocusNames=AM1_4415;
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Acaryochloris.
OX NCBI_TaxID=329726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017;
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M.,
RA Shimada Y., Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J.,
RA Mimuro M., Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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; CP000828; ABW29392.1; -; Genomic_DNA.
DR RefSeq; YP_001518709.1; NC_009925.1.
DR ProteinModelPortal; B0CEZ5; -.
DR STRING; 329726.AM1_4415; -.
DR EnsemblBacteria; ABW29392; ABW29392; AM1_4415.
DR GeneID; 5683217; -.
DR KEGG; amr:AM1_4415; -.
DR PATRIC; 20622916; VBIAcaMar40141_4079.
DR eggNOG; COG0165; -.
DR HOGENOM; HOG000242744; -.
DR KO; K01755; -.
DR OMA; KEGIFDA; -.
DR ProtClustDB; PRK00855; -.
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.
FT CHAIN 1 476 Argininosuccinate lyase.
FT /FTId=PRO_0000335822.
SQ SEQUENCE 476 AA; 52917 MW; 42093BB483AD1EC1 CRC64;
MTSSPVPPTN SSDSSDSKVW SQRFESALNP VIAAFNASIH FDIALIEYDL TGSQAHVQML
AHSGIISQAE ADAIDQGLEA IRQEYRQGQF QPGIEAEDIH FAVENRLIEL IGDTGKKLHT
GRSRNDQVGT DLRLYLHDQI LQVQTLIRNW QQALVILASD HVQTLIPGYT HLQRAQPISL
AHHLLAYFEM AERDWQRLRE IDRRVNVSPL GLGALAGTPF PIDRQYTADK LGFADLYRNS
LDGVSDRDFA IEFLCAASLI MVHLSRFSEE VILWASEEFG FIKLKDSCAT GSSIMPQKKN
PDVPELVRGK SGRVFGHLQS LLVVMKGLPL AYNKDLQEDK EAIFDGVTTI KACLEAMTIL
VAEGLEFQTP RLESAVGEDF SNATDVADYL SKQGVPFREA YNIVGAVVKT CLSQNKLLKD
LTLEEWQQFH PQFADDIYSA ISPRQVVAVR NSFGGTGFTQ VQNALEQAKT LLSQSK
//
