ARLY_SYNP6
ID ARLY_SYNP6 Reviewed; 466 AA.
AC Q5N1K1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Argininosuccinate lyase {ECO:0000255|HAMAP-Rule:MF_00006};
DE Short=ASAL {ECO:0000255|HAMAP-Rule:MF_00006};
DE EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006};
DE AltName: Full=Arginosuccinase {ECO:0000255|HAMAP-Rule:MF_00006};
GN Name=argH {ECO:0000255|HAMAP-Rule:MF_00006}; OrderedLocusNames=syc1629_c;
OS Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS nidulans).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=269084;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT Synechococcus elongatus PCC 6301 chromosome: gene content and
RT organization.";
RL Photosyn. Res. 93:55-67(2007).
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; Evidence={ECO:0000255|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. {ECO:0000255|HAMAP-
CC Rule:MF_00006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00006}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000255|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; AP008231; BAD79819.1; -; Genomic_DNA.
DR RefSeq; WP_011243939.1; NC_006576.1.
DR AlphaFoldDB; Q5N1K1; -.
DR SMR; Q5N1K1; -.
DR STRING; 269084.syc1629_c; -.
DR EnsemblBacteria; BAD79819; BAD79819; syc1629_c.
DR KEGG; syc:syc1629_c; -.
DR eggNOG; COG0165; Bacteria.
DR OMA; KKNPDVF; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001175; 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; 1.10.275.10; -; 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 PANTHER; PTHR43814; PTHR43814; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR00838; argH; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase.
FT CHAIN 1..466
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137838"
SQ SEQUENCE 466 AA; 51822 MW; 9B41900A8F2BC851 CRC64;
MTQAAAPQPW SDRFETALHP AIVVFNASIG FDLALIEYDL TGSQAHAQML AEQDIISREE
GEAIVAGLEQ IRSEYRTGQF QPGLDAEDVH FAVERRLTEL LGDVGKKLHT ARSRNDQVGT
DTRLYLRDRV DHIRQQLRDY QRVLLSQAEQ HLETLIPGYT HLQRAQPLSL AHHLHAYLEM
AERDWERLGD LRKRLNTSPL GAGALAGTTF PIDRQRTAAL LGFERIYANS LDAVSDRDSL
VEFLAAASLI MVHLSRLAEE VILWASEEFR FVRLSDRCAT GSSITPQKKN PDVPELVRGK
TGRVFGHLQA LLVVLKGLPL AYNKDLQEDK EGLFDAVQTV ESCLEAMTIL FAEGLSFQPD
RLAAAVEADF SNATDVADYL AARGVPFREA YNLVGRVVRT CLEQGKLLKD LSLAEWQALH
PQFEADIYTA IAPQQVVAAR NSLGGTGFEQ VRSALASVRQ RLEATC