ARLY_MARSD
ID ARLY_MARSD Reviewed; 460 AA.
AC C6BTR8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=Desal_1786;
OS Maridesulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIMB 8403 /
OS VKM B-1763) (Desulfovibrio salexigens).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Maridesulfovibrio.
OX NCBI_TaxID=526222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14822 / DSM 2638 / NCIMB 8403 / VKM B-1763;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Wall J.D., Arkin A.P., Dehal P., Chivian D., Giles B., Hazen T.C.;
RT "Complete sequence of Desulfovibrio salexigens DSM 2638.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP001649; ACS79848.1; -; Genomic_DNA.
DR RefSeq; WP_015851664.1; NC_012881.1.
DR AlphaFoldDB; C6BTR8; -.
DR SMR; C6BTR8; -.
DR STRING; 526222.Desal_1786; -.
DR PRIDE; C6BTR8; -.
DR EnsemblBacteria; ACS79848; ACS79848; Desal_1786.
DR KEGG; dsa:Desal_1786; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_7; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 751464at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000002601; 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; IPR020557; Fumarate_lyase_CS.
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.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase;
KW Reference proteome.
FT CHAIN 1..460
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000201695"
SQ SEQUENCE 460 AA; 51159 MW; F0C1BC706EBDE181 CRC64;
MADNKLWGGR FAAKTAQSVE DYTESVSYDQ NLYREDISGS QAHAKMLAEQ GVLTAEEAEI
LVKGLDQVLE EIESGKFEWK KEMEDLHMNI ESRLTEIVGP VGGKLHTGRS RNDQVATDFR
LHVLRSLEAW KTALEKLIAS FTAKADANRE VLLPGYTHLQ PAQPVSLAHH MLAYAWMFKR
DHSRVVDCIN RANVCPLGAA ALAGTTYPLK PATSAKYLGM EDTFRNSLDA VSDRDFVMEA
MFTGSLIMTH LSRICEELII WANPCFGFIK LPDEFSTGSS IMPQKKNPDV CELMRGKTGR
VYGDLFSLMT TCKGLPLAYN RDMQEDKEPF FDCDKTVHAS VVIMADMMDA MGFNPANMES
ALKKGFLNAT ELADYLVGKG IPFREAHHIT GSAVAKAEAE SRGLEDMSLE ELKTFSDKIE
EDVFEVLSYE AAVRRRVSPG STGPESVDSQ IAELKAWLKK