ID Q59R31_CANAL Unreviewed; 468 AA.
AC Q59R31; Q3MP00;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE RecName: Full=Arginosuccinase {ECO:0000256|ARBA:ARBA00032749};
GN Name=ARG4 {ECO:0000313|CGD:CAL0000190527,
GN ECO:0000313|EMBL:AOW30699.1};
GN OrderedLocusNames=CAALFM_C703570WA {ECO:0000313|EMBL:AOW30699.1},
GN orf19.13981 {ECO:0000313|CGD:CAL0000190527};
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561 {ECO:0000313|EMBL:AOW30699.1, ECO:0000313|Proteomes:UP000000559};
RN [1] {ECO:0000313|EMBL:AOW30699.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2] {ECO:0000313|EMBL:AOW30699.1, ECO:0000313|Proteomes:UP000000559}
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=17419877; DOI=.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3] {ECO:0000313|EMBL:AOW30699.1, ECO:0000313|Proteomes:UP000000559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876 {ECO:0000313|Proteomes:UP000000559};
RX PubMed=24025428; DOI=.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000256|ARBA:ARBA00010755}.
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DR EMBL; CP017629; AOW30699.1; -; Genomic_DNA.
DR RefSeq; XP_712142.1; XM_707049.1.
DR AlphaFoldDB; Q59R31; -.
DR SMR; Q59R31; -.
DR STRING; 237561.Q59R31; -.
DR EnsemblFungi; C7_03570W_A-T; C7_03570W_A-T-p1; C7_03570W_A.
DR GeneID; 3646237; -.
DR KEGG; cal:CAALFM_C703570WA; -.
DR CGD; CAL0000190527; ARG4.
DR VEuPathDB; FungiDB:C7_03570W_A; -.
DR eggNOG; KOG1316; Eukaryota.
DR HOGENOM; CLU_027272_2_1_1; -.
DR InParanoid; Q59R31; -.
DR OMA; DFAIEFC; -.
DR OrthoDB; 2722228at2759; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000000559; Chromosome 7.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IMP:CGD.
DR GO; GO:0006526; P:arginine biosynthetic process; IMP:CGD.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR CDD; cd01359; Argininosuccinate_lyase; 1.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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 NCBIfam; TIGR00838; argH; 1.
DR PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:AOW30699.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000559}.
FT DOMAIN 17..312
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 375..443
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 468 AA; 52816 MW; F2B04EA318F8135E CRC64;
MSQQQDKQPS ENKLWGGRFT GATDPLMDLY NASLPYDKVM YDADLTGTKV YTQGLNKLGL
ITTEELHLIH QGLEQIRQEW HDNKFIIKAG DEDIHTANER RLGEIIGKNI SGKVHTGRSR
NDQVATDMRI FVRESLLNLS KILHQFITAI LERAHKEIDV LMPGYTHLQK AQPIRWAHWL
SSYATYFTED YKRLQEIITR VNQSPLGSGA LAGHPYGIDR EFLAKGLGFD GVIGNSLTAV
SDRDFVVESL FWSTLFMNHI SRFSEDLIIY SSGEFGFIKL ADAYSTGSSL MPQKKNPDSL
ELLRGKSGRV FGQLSGFLMS IKSIPSTYNK DMQEDKEPLF DALTTVEHSI LIATGVISTL
SIDKQNMEKA LTMDMLATDL ADYLVRKGVP FRETHHISGE CVRKAEEEKL SGIDQLSFEQ
FQQIDSRFEK DVMETFDFEA SVERRDAIGG TAKSAVLKQL ENLKSILS
//
