ARLY_CORGL
ID ARLY_CORGL Reviewed; 477 AA.
AC O88101;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 143.
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};
GN OrderedLocusNames=Cgl1401, cg1588;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613;
RA Park M.Y., Chun J.Y., Ko S.-Y., Lee M.-S.;
RT "Molecular cloning of the arginine biosynthetic genes from Corynebacterium
RT glutamicum.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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; AF048764; AAC24811.1; -; Genomic_DNA.
DR EMBL; AF049897; AAC24819.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98794.1; -; Genomic_DNA.
DR EMBL; BX927152; CAF21412.1; -; Genomic_DNA.
DR RefSeq; NP_600620.1; NC_003450.3.
DR RefSeq; WP_011014337.1; NC_006958.1.
DR AlphaFoldDB; O88101; -.
DR SMR; O88101; -.
DR STRING; 196627.cg1588; -.
DR KEGG; cgb:cg1588; -.
DR KEGG; cgl:Cgl1401; -.
DR PATRIC; fig|196627.13.peg.1370; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_2_11; -.
DR OMA; KKNPDVF; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000000582; 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..477
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137764"
FT CONFLICT 10..13
FT /note="ALWG -> GCGP (in Ref. 1; AAC24811/AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 41..66
FT /note="DVLASKAHAKVLHQADLLSDEDLATM -> HLHAPRAHTMVLFRAGLLTEEQ
FT RDGL (in Ref. 1; AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 72..75
FT /note="QLGK -> SLAQ (in Ref. 1; AAC24811/AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="T -> S (in Ref. 1; AAC24811/AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 86..87
FT /note="PS -> VT (in Ref. 1; AAC24811/AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..95
FT /note="GAM -> AAL (in Ref. 1; AAC24811/AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="K -> E (in Ref. 1; AAC24811/AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="K -> E (in Ref. 1; AAC24811/AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="L -> Q (in Ref. 1; AAC24811/AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="G -> R (in Ref. 1; AAC24811/AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="G -> R (in Ref. 1; AAC24811/AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="I -> L (in Ref. 1; AAC24811/AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="L -> V (in Ref. 1; AAC24811/AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 319..321
FT /note="KAQ -> EAH (in Ref. 1; AAC24811/AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 326..328
FT /note="NRD -> SRV (in Ref. 1; AAC24811/AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="V -> L (in Ref. 1; AAC24811/AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="V -> L (in Ref. 1; AAC24811/AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 361..369
FT /note="TERMRELAP -> DQPDADLDR (in Ref. 1; AAC24811/
FT AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="A -> P (in Ref. 1; AAC24811/AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 379..390
FT /note="AEWMVRQGVPFR -> RERDRQGGSNSG (in Ref. 1; AAC24811/
FT AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 396..419
FT /note="SGACVRIAESRGVDLIDLTDEELS -> PARSGGSCGPSPGSGPYRSHRRRT
FT R (in Ref. 1; AAC24811/AAC24819)"
FT /evidence="ECO:0000305"
FT CONFLICT 425..465
FT /note="LTPEVREVLTIDGAVASRATRGGTAGVRVAEQRARVDAAST -> PDPRGTG
FT SAHHSWCSGFPSNRRWNRARAGCGATRTCRCRKY (in Ref. 1; AAC24811/
FT AAC24819)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 51042 MW; 06364CA7FEE80E9B CRC64;
MEQHGTNEGA LWGGRFSGGP SEAMFALSVS THFDWVLAPY DVLASKAHAK VLHQADLLSD
EDLATMLAGL DQLGKDVADG TFGPLPSDED VHGAMERGLI DRVGPEVGGR LRAGRSRNDQ
VATLFRMWVR DAVRDIALGT TELVDALSAQ AKAHAGAIMP GKTHFQAAQP VLLAHQLLAH
AQPLLRDIDR IRDLDKRLAV SPYGSGALAG SSLKLNPEAI AEELGFDSAA DNSIDATSSR
DFASETAFVL AQLAVDMSRL AEEIIAWCTP EFGYITLSDS WSTGSSIMPQ KKNPDVAELT
RGKSGRLIGN LTGLLATLKA QPLAYNRDLQ EDKEPIVDSV AQLNLLLPAM TGLVSTLTFN
TERMRELAPA GFTLATDLAE WMVRQGVPFR EAHEASGACV RIAESRGVDL IDLTDEELSG
VDARLTPEVR EVLTIDGAVA SRATRGGTAG VRVAEQRARV DAASTAHAEW ARAGVRR
