ID A0A0F7FQU8_9ACTN Unreviewed; 477 AA.
AC A0A0F7FQU8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE Short=ASAL {ECO:0000256|HAMAP-Rule:MF_00006};
DE EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE AltName: Full=Arginosuccinase {ECO:0000256|HAMAP-Rule:MF_00006};
GN Name=argH {ECO:0000256|HAMAP-Rule:MF_00006};
GN ORFNames=SXIM_04160 {ECO:0000313|EMBL:AKG41800.1};
OS Streptomyces xiamenensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=408015 {ECO:0000313|EMBL:AKG41800.1, ECO:0000313|Proteomes:UP000034034};
RN [1] {ECO:0000313|Proteomes:UP000034034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A01550 {ECO:0000313|Proteomes:UP000034034};
RA Xu J.;
RT "Complete genome sequence of a mangrove-derived Streptomyces xiamenensis.";
RL Submitted (FEB-2015) 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;
CC Evidence={ECO:0000256|ARBA:ARBA00000985, ECO:0000256|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.
CC {ECO:0000256|ARBA:ARBA00004941, ECO:0000256|HAMAP-Rule:MF_00006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00006}.
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DR EMBL; CP009922; AKG41800.1; -; Genomic_DNA.
DR RefSeq; WP_030727281.1; NZ_CP009922.3.
DR AlphaFoldDB; A0A0F7FQU8; -.
DR STRING; 408015.SXIM_04160; -.
DR KEGG; sxi:SXIM_04160; -.
DR PATRIC; fig|408015.6.peg.444; -.
DR HOGENOM; CLU_027272_2_3_11; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000034034; 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; 1.10.40.30; 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00006};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_00006}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000313|EMBL:AKG41800.1}.
FT DOMAIN 17..310
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 373..439
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 477 AA; 51269 MW; BEFAE522FDDC345E CRC64;
MTHTAPNDVK LWGGRFADGP AAALEKLSAS VHFDWRLAPY DIAGSRAHAR VLHRAGLLTD
DELERMLAGL DRLAADVADG SFTGTIADED VHTALERGLL ERLGPDLGGK LRAGRSRNDQ
VATLFRMYLR DHARIIGALI ADLQEALVGL AEAHPEVAMP GRTHLQHAQP VLFAHHVLAH
FQALSRDAQR LRQWDERTAV SPYGSGALAG SSLGLDPQAV AADLGFEGGS VANSIDGTAS
RDFVAEFAFI TAMIGVDLSR IAEEIIIWNT KEFSFVTLHD AFSTGSSIMP QKKNPDIAEL
ARGKSGRLIG NLTGLLATLK ALPLAYNRDL QEDKEPVFDS CDQLEILLPA FTGMLATLTV
HRERMEELAP AGFSLATDIA EWLVKQGVPF REAHESAGEC VKVCEAAGIE LDELTDEQFA
KISPRLTPQV RTVLNVPGAL AARDARGGTA PSAVAVQLAE AKADLTVQRE WSGPAVV
//
