ARLY_METC4
ID ARLY_METC4 Reviewed; 463 AA.
AC B7KW75;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=Mchl_3612;
OS Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium
OS extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=440085;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM4 / NCIMB 13688;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Marx C., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium chloromethanicum
RT CM4.";
RL Submitted (DEC-2008) 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; CP001298; ACK84432.1; -; Genomic_DNA.
DR RefSeq; WP_015951679.1; NC_011757.1.
DR AlphaFoldDB; B7KW75; -.
DR SMR; B7KW75; -.
DR EnsemblBacteria; ACK84432; ACK84432; Mchl_3612.
DR KEGG; mch:Mchl_3612; -.
DR HOGENOM; CLU_027272_2_3_5; -.
DR OMA; KKNPDVF; -.
DR BioCyc; MEXT440085:MCHL_RS17585-MON; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000002385; 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.
FT CHAIN 1..463
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000116331"
SQ SEQUENCE 463 AA; 49706 MW; 113267E576665A69 CRC64;
MSNRMWGGRF ASGPAEIMEE INASIGFDRR LASQDIRGSL AHVAMLGSQG ILPAEDVAAI
EAGLKSVEAE IARGEFVFRR ELEDIHMAVE SRLTEIVGPA AGRLHTARSR NDQVATDMRL
WVRDTLDALD AQVADLQRAL AETAVKHAGT VMPGFTHLQS AQPVTFGHHC LAYVEMLARD
RGRFRDARAR LNECPLGAAA LAGTSFPIDR HATAAALGFD RPTANSLDSV ADRDFALESL
SAASICAVHL SRFAEELVVW TSAQFGFVRL SDGFTTGSSI MPQKRNPDAA ELVRAKAGRI
IGALTGLLIV MKGLPLAYSK DMQEDKEGTF DALQSLSLCL AAMAGMVRDL EPVAETLKRA
AGSGYATATD LADWLVRELN MPFRQAHHVT GRVVAAASER GIGLEELSLQ DMQAVEAGIT
DAVFAVLGVE NSVASRTSYG GTAPDNVRRQ AEGWLEKLGP VEK