ID A6RDU7_AJECN Unreviewed; 471 AA.
AC A6RDU7;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Arginosuccinase {ECO:0000256|ARBA:ARBA00032749};
GN ORFNames=HCAG_07805 {ECO:0000313|EMBL:EDN11352.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN11352.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000256|ARBA:ARBA00010755}.
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DR EMBL; CH476663; EDN11352.1; -; Genomic_DNA.
DR AlphaFoldDB; A6RDU7; -.
DR STRING; 339724.A6RDU7; -.
DR VEuPathDB; FungiDB:HCAG_07805; -.
DR HOGENOM; CLU_027272_2_1_1; -.
DR OMA; DFAIEFC; -.
DR OrthoDB; 2722228at2759; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000009297; Unassembled WGS sequence.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:InterPro.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
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:EDN11352.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009297}.
FT DOMAIN 20..316
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 379..446
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 471 AA; 52323 MW; 0A30A1269C7637E2 CRC64;
MASQNQQTAS GAVAGKLWGG RFTGATDPLM VAYNESIYFD RAFYAQDIAG SIAFARANVT
TGILTKDEFG SIETGLRKVL EEWRTGVFKI VPGIDEDIHT ANERRLGEII GKDIAGKLHT
GRSRNDQVAT DLRLWLRDEL RVIETYLVDL LTTIADRAKN DIDYVIPGYT HLQRGQPVRW
SHWMLSYGSF FMNDLERLRE VIKHVNRSPL GCGALSGNAF GIDREAMAKE LGFDGLIPNS
MSAVGDRDFI LETMQWGSSL MLHISRWSED LIVYGTTEFG FVRLSDAYTT GSSLMPQKKN
SDSLELLRGK CGRIFGGMAG LMMTIKGIPS TYNKDLQESV EPLLEHVKTL KDSLLIATRV
LSTLTVFPDK MRQALTPDML ATDLAEYLVR KGLPFRETHH IAGRVVALAE NQGIPMDKLT
LAQLQSVDNR FGDDVLEVFD YERSVEMKAA IGGTSRSAVL EQIATLRKAL G
//
